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83 results on '"H. Uedaira"'

1. Contributory presentations/posters

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N. Manoj, V. R. Srinivas, A. Surolia, M. Vijayan, K. Suguna, R. Ravishankar, R. Schwarzenbacher, K. Zeth, null Diederichs, G. M. Kostner, A. Gries, P. Laggner, R. Prassl, null Madhusudan, Pearl Akamine, Nguyen-huu Xuong, Susan S. Taylor, M. Bidva Sagar, K. Saikrishnan, S. Roy, K. Purnapatre, P. Handa, U. Varshney, B. K. Biswal, N. Sukumar, J. K. Mohana Rao, A. Johnson, Vasantha Pattabhi, S. Sri Krishna, Mira Sastri, H. S. Savithri, M. R. N. Murthy, Bindu Pillai, null Kannan, M. V. Hosur, Mukesh Kumar, Swati Patwardhan, K. K. Kannan, B. Padmanabhaa, S. Sasaki-Sugio, M. Nukaga, T. Matsuzaki, S. Karthikevan, S. Sharma, A. K. Sharma, M. Paramasivam, P. Kumar, J. A. Khan, S. Yadav, A. Srinivasan, T. P. Singh, S. Gourinath, Neelima Alam, A. Srintvasan, Vikas Chandra, Punit Kaur, Ch. Betzel, S. Ghosh, A. K. Bera, S. Bhattacharya, S. Chakraborty, A. K. Pal, B. P. Mukhopadhyay, I. Dey, U. Haldar, Asok Baneriee, Jozef Sevcik, Adriana Solovicova, K. Sekar, M. Sundaralingam, N. Genov, Dong-cai Liang, Tao Jiang, Ji-ping Zhang, Wen-rui Chang, Wolfgang Jahnke, Marcel Blommers, S. C. Panchal, R. V. Hosur, Bindu Pillay, Puniti Mathur, S. Srivatsun, Ratan Mani Joshi, N. R. Jaganathan, V. S. Chauhan, H. S. Atreya, S. C. Sahu, K. V. R. Chary, Girjesh Govil, Elisabeth Adjadj, Éric Quinjou, Nadia Izadi-Pruneyre, Yves Blouquit, Joël Mispelter, Bernadette Heyd, Guilhem Lerat, Philippe Milnard, Michel Desmadreil, Y. Lin, B. D. Nageswara Rao, Vidva Raghunathan, Mei H. Chau, Prashant Pesais, Sudha Srivastava, Evans Coutinho, Anil Saran, Leizl F. Sapico, Jayson Gesme, Herbert Lijima, Raymond Paxton, Thamarapu Srikrishnan, C. R. Grace, G. Nagenagowda, A. M. Lynn, Sudha M. Cowsik, Sarata C. Sahu, S. Chauhan, A. Bhattacharya, G. Govil, Anil Kumar, Maurizio Pellecchia, Erik R. P. Zuiderweg, Keiichi Kawano, Tomoyasu Aizawa, Naoki Fujitani, Yoichi Hayakawa, Atsushi Ohnishi, Tadayasu Ohkubo, Yasuhiro Kumaki, Kunio Hikichi, Katsutoshi Nitta, V. Rani Parvathy, R. M. Kini, Takumi Koshiba, Yoshihiro Kobashigawa, Min Yao, Makoto Demura, Astushi Nakagawa, Isao Tanaka, Kunihiro Kuwajima, Jens Linge, Seán O. Donoghue, Michael Nilges, G. Chakshusmathi, Girish S. Ratnaparkhi, P. K. Madhu, R. Varadarajan, C. Tetreau, M. Tourbez, D. Lavalette, M. Manno, P. L. San Biagio, V. Martorana, A. Emanuele, S. M. Vaiana, D. Bulone, M. B. Palma-Vittorelli, M. U. Palma, V. D. Trivedi, S. F. Cheng, W. J. Chien, S. H. Yang, S. Francis, D. K. Chang, Renn Batra, Michael A. Geeves, Dietmar J. Manstein, Joanna Trvlska, Pawel Grochowski, Maciej Geller, K. Ginalski, P. Grochowski, B. Lesyng, P. Lavalette, Y. Blouquit, D. Roccatano, A. Amadei, A. Di Nola, H. J. C. Berendsen, Bosco Ho, P. M. G. Curmi, H. Berry, D. Lairez, E. Pauthe, J. Pelta, V. Kothekar, Shakti Sahi, M. Srinivasan, Anil K. Singh, Kartha S. Madhusudnan, Fateh S. Nandel, Harpreet Kaur, Balwinder Singh, D. V. S. Jain, K. Anton Feenstra, Herman J. C. Berendsen, F. Tama, Y. -H. Sanejouand, N. Go, Deepak Sharma, Sunita Sharma, Santosh Pasha, Samir K. Brahmachari, R. Viiavaraghavan, Jyoti Makker, Sharmisllia Dey, S. Kumar, G. S. Lakshmikanth, G. Krishnamoorthy, V. M. Mazhul, E. M. Zaitseva, Borys Kierdaszuk, J. Widengren, B. Terry, Ü. Mets, R. Rigler, R. Swaminathan, S. Thamotharan, N. Yathindra, Y. Shibata, H. Chosrowjan, N. Mataga, I. Morisima, Tania Chakraharty, Ming Xiao, Roger Cooke, Paul Selvin, C. Branca, A. Faraone, S. Magazù, G. Maisano, P. Migliardo, V. Villari, Digambar V. Behere, M. Sharique Zahida Waheed Deva, M. Brunori, F. Cutruzzolà, Q. H. Gibson, C. Savino, C. Travaglini-Allocatelli, B. Vallone, Swati Prasad, Shyamalava Mazumdar, Samaresh Mitra, P. Soto, R. Fayad, I. E. Sukovataya, N. A. Tyulkova, Sh. V. Mamedov, B. Aktas, M. Canturk, B. Aksakal, R. Yilgin, K. I. Bogutska, N. S. Miroshnichenko, S. Chacko, M. DiSanto, J. A. Hypolite, Y-M. Zheng, A. J. Wein, M. Wojciechowski, T. Grycuk, J. Antosiewicz, Marc A. Ceruso, Alfredo Di Nola, Subhasis Bandvopadhvay, Bishnu P. Chatterjee, Devapriva Choudhury, Andrew Thompson, Vivian Stojanoff, Jerome Pinkner, Scott Hultgren, Stefan Khight, Delphine Flatters, Julia Goodfellow, Fumi Takazawatt, Minoru Kanehisa, Masaki Sasai, Hironori Nakamura, Wang Bao Han, Yuan Zheng, Wang Zhi Xin, Pan xin Min, Vlnod Bhakuni, Sangeeta Kulkarni, Atta Ahmad, Koodathingal Prakash, Shashi Prajapati, Alexey Surin, Tomoharu Matsumoto, Li Yang, Yuki Nakagawa, Kazumoto Kimura, Yoshiyuki Amemiya, Gennady V. Semisotnov, Hiroshi Kihara, Saad Tayyab, Salman Muzammil, Yogesh Kumar, Vinod Bhakuni, Monica Sundd, Suman Kundu, M. V. Jagannadham, Medicherla V. Jagannadham, Bina Chandani, Ruby Dhar, Lalankumar Sinha, Deepti Warrier, Sonam Mehrotra, Purnima Khandelwal, Subhendu Seth, Y. U. Sasidhar, C. Ratna Prabha, Arun Gidwani, K. P. Madhusudan, Akira R. Kinjo, Ken Nishikawa, Suvobrata Chakravarty, Raghavan Varadarajan, K. Noyelle, P. Haezebrouck, M. Joniau, H. Van Dael, Sheffali Dash, Indra Brata Jha, Rajiv Bhat, Prasanna Mohanty, A. K. Bandyopadhyay, H. M. Sonawat, Ch. Mohan Rao, Siddhartha Datta, K. Rajaraman, B. Raman, T. Ramakrishna, A. Pande, J. Pande, S. Betts, N. Asherie, O. Ogun, J. King, G. Benedek, I. V. Sokolova, G. S. Kalacheva, Masashi Sonoyama, Yasunori Yokoyama, Kunihiro Taira, Shigeki Mitaku, Chicko Nakazawal, Takanori Sasakil, Yuri Mukai, Naoki Kamo, Seema Dalal, Lynne Regan, Shigeki Mituku, Mihir Roychoudhury, Devesh Kumar, Dénes Lőrinczv, Franciska Könczöl, László Farkas, Joseph Belagyi, Christoph Schick, Christy A. Thomson, Vettai S. Ananthanarayanan, E. G. Alirzayeva, S. N. Baba-Zade, M. Michael Gromiha, M. Oobatake, H. Kono, J. An, H. Uedaira, A. Sarai, Kazufumi Takano, Yuriko Yamagata, Katsuhide Yutani, Gouri S. Jas, Victor Muñoz, James Hofrichter, William A. Eaton, Jonathan Penoyar, Philip T. Lo Verde, J. Kardos, Á. Bódi, I. Venekei, P. Závodszky, L. Gráf, András Szilágyi, Péter Závodszky, R. D. Allan, J. Walshaw, D. N. Woolfson, Jun Funahashi, Savan Gupta, M. Mangoni, P. Roccatano, Gosu Ramachandraiah, Nagasuma R. Chandra, Barbara Ciani, Derek N. Woolfson, Usha B. Nair, Kanwal J. Kaur, Dinakar M. Salunke, Chittoor P. Swaminathan, Avadhesha Surolia, A. Pramanik, P. Jonasson, G. Kratz, O. T. Jansson, P. -Å. Nygren, S. Ståhl, K. Ekberg, B. -L. Johansson, S. Uhlén, M. Uhlén, H. Jörnvall, J. Wahren, Karin Welfle, Rolf Misselwitz, Wolfgang Höhne, Heinz Welfle, L. G. Mitskevich, N. V. Fedurkina, B. I. Kurganov, Gotam K. Jarori, Haripada Maity, J. Guharay, B. Sengupta, P. K. Sengupta, K. Sridevi, S. R. Kasturi, S. P. Gupta, Gunjan Agarwal, Suzanne Kwong, Robin W. Briehl, O. I. Ismailova, N, A. Tyulkova, C. Hariharan, D. Pines, E. Pines, M. Zamai, R. Cohen-Luria, A. Yayon, A. H. Parola, M. J. Padya, G. A. Spooner, D. N. Woolfeon, Panchan Bakshi, D. K. Bharadwaj, U. Sharma, N. Srivastava, R. Barthwal, N. R. Jagannathan, Keiko Matsuda, Takaaki Nishioka, Nobuhiro Go, T. Aita, S. Urata, Y. Husimi, Mainak Majumder, Nicola G. A. Abrescia, Lucy Malinina, Juan A. Subirana, Juan Aymami, Ramón Eritxa, Miquel Coll, B. J. Premraj, R. Thenmalarchelvi, P. Satheesh Kumar, N. Gautham, Lou -Sing Kan, null Ming-Hou, Shwu-Bin Lin, Tapas Sana, Kanal B. Roy, N. Bruant, D. Flatters, R. Lavery, D. Genest, Remo Rons, Heinz Sklenar, Richard Lavery, Sudip Kundu, Dhananjay Bhattacharyya, Debashree Bandyopadhyay, Ashoke Ranjan Thakur, Rabi Majumdar, F. Barceló, J. Portugal, Sunita Ramanathan, B. J. Rao, Mahua Gliosli, N. Vinay Kumar, Umesh Varshney, Shashank S. Pataskar, R. Sarojini, S. Selvasekarapandian, P. Kolandaivel, S. Sukumar, P. Kolmdaivel, Motilal Maiti, Anjana Sen, Suman Das, Elisa Del Terra, Chiara Suraci, Silvia Diviacco, Franco Quadrifoglio, Luigi Xodo, Arghya Ray, G. Karthikeyan, Kandala V. R. Chary, Basuthkar J. Rao, Anwer Mujeeb, Thomas L. James, N. Kasyanenko, E. E. F. Haya, A. Bogdanov, A. Zanina, M. R. Bugs, M. L. Cornélio, M. Ye. Tolstorukov, Nitish K. Sanval, S. N. Tiwari, Nitish K. Sanyal, Mihir Roy Choudhury, P. K. Patel, Neel S. Bhavesh, Anna Gabrielian, Stefan Wennmalm, Lars Edman, Rudolf Rigler, B. Constantinescu, L. Radu, I. Radulcscu, D. Gazdaru, Sebastian Wärmländer, Mikael Leijon, Setsuyuki Aoki, Takao Kondo, Masahiro Ishiura, V. A. Pashinskaya, M. V. Kosevich, V. S. Shelkovsky, Yu. P. Blagoy, Ji-hua Wang, R. Malathi, K. Chandrasekhar, E. R. Kandimalla, S. Agrawal, V. K. Rastogi, M. Alcolea Palafox, Chatar Singh, A. D. Beniaminov, S. A. Bondarenko, E. M. Zdobnov, E. E. Minyat, N. B. Ulyanov, V. I. Ivanov, J. S. Singh, Kailas D. Sonawane, Henri Grosjean, Ravindra Tewari, Uddhavesh B. Sonavane, Annie Morin, Elizabeth A. Doherty, Jennifer A. Doudna, H. Tochio, S. Sato, H. Matsuo, M. Shirakawa, Y. Kyogoku, B. Javaram, Surjit B. Dixit, Piyush Shukla, Parul Kalra, Achintya Das, Kevin McConnell, David L. Beveridge, W. H. Sawyer, R. Y. S. Chan, J. F. Eccelston, Yuling Yan, B. E. Davidson, Eimer Tuite, Bengt Norden, Peter Nielsen, Masayuki Takahashi, Anirban Ghosh, Manju Bansal, Frauke Christ, Hubert Thole, Wolfgang Wende, Alfred Pingoud, Vera Pingoud, Pratibha Mehta Luthra, Ramesh Chandra, Ranjan Sen, Rodney King, Robert Weisberg, Olaf F. A. Larsen, Jos Berends, Hans A. Heus, Cornelis W. Hilbers, Ivo H. M. van Stokkum, Bas Gobets, Rienk van Grondelle, Herbert van Amerongen, HE. Sngrvan, Yu. S. Babayan, N. V. Khudaverdian, M. Gromiha, F. Pichierri, M. Aida, P. Prabakaran, K. Sayano, Saulius Serva, Eglė Merkienė, Giedrius Vilkaitis, Elmar Weinhold, Saulius Klimašauskas, Eleonora Marsich, Antonella Bandiera, Giorgio Manzini, G. Potikyan, V. Arakelyan, Yu. Babayan, Alex Ninaber, Julia M. Goodfellow, Yoichiro Ito, Shigeru Ohta, Yuzuru Husimi, J. Usukura, H. Tagami, H. Aiba, Mougli Suarez, Elia Nunes, Deborah Keszenman, E. Carmen Candreva, Per Thyberg, Zeno Földes-Papp, Amita Joshi, Dinesh Singh, M. R. Rajeswari, null Ira, M. Pregetter, H. Amenitsch, J. Chapman, B. N. Pandev, K. P. Mishra, E. E. Pohl, J. Sun, I. I. Agapov, A. G. Tonevitsky, P. Pohl, S. M. Dennison, G. P. Gorbeako, T. S. Dynbko, N. Pappavee, A. K. Mishra, Prieto Manuel, Almeida Rodrigo, Loura Luis, L. Ya. Gendel, S. Przestalski, J. Kuczera, H. Kleszczyńska, T. Kral, E. A. Chernitsky, O. A. Senkovich, V. V. Rosin, Y. M. Allakhverdieva, G. C. Papageorgiou, R. A. Gasanov, Calin Apetrei, Tudor Savopol, Marius Balea, D. Cucu, D. Mihailescu, K. V. Ramanathan, Goran Bačić, Nicolas Sajot, Norbert Garnier, Serge Crouzy, Monique Genest, Z. S. Várkonyi, O. Zsiros, T. Farkas, Z. Combos, Sophie Cribier, I. F. Fraceto, S. Schreier, A. Spisni, F. de Paula, F. Sevšek, G. Gomišček, V. Arrigler, S. Svetina, B. Žekš, Fumimasa Nomura, Miki Nagata, Kingo Takiguchi, Hirokazu Hotani, Lata Panicker, P. S. Parvathanathan, A. Ishino, A. Saitoh, H. Hotani, K. Takiguchi, S. Afonin, A. Takahashi, Y. Nakato, T. Takizawa, Dipti Marathe, Kent Jørgensen, Satinder S. Rawat, R. Rukmini, Amitabha Chattopadhyay, M. Šentiurc, J. Štrancar, Z. Stolič, K. Filipin, S. Pečar, S. C. Biswas, Satyen Sana, Anunay Samanta, Koji Kinoshita, Masahito Yamazaki, Tetsuhiko Ohba, Tai Kiuchi, null Yoshitoshi, null Kamakura, Akira Goto, Takaaki Kumeta, Kazuo Ohki, I. P. Sugar, T. E. Thompson, K. K. Thompson, R. L. Biltonen, Y. Suezaki, H. Ichinose, M. Akivama, S. Matuoka, K. Tsuchihashi, S. Gasa, P. Mattjus, J. G. Molotkovsky, H. M. Pike, R. E. Brown, Ashish Arora, Jörg H. Kleinschmidt, Lukas K. Tamm, O. G. Luneva, K. E. Kruglyakova, V. A. Fedin, O. S. Kuptsoya, J. W. Borst, N. V. Visser, A. J. W. G. Visser, T. S. Dyubko, Toshihiko Ogihara, Kiyoshi Mishima, A. L. Shvaleva, N. Č. Radenović, P. M. Minić, M. G. Jeremić, Č. N. Radenović, T. F. Aripov, E. T. Tadjibaeva, O. N. Vagina, M. V. Zamaraeva, B. A. Salakhutdinov, A. Cole, M. Poppofl, C. Naylor, R. Titball, A. K. Basak, J. T. Eaton, C. E. Naylor, N. Justin, D. S. Moss, R. W. Titball, F. Nomura, M. Nagata, S. Ishjkawa, S. Takahashi, Kaoru Obuchi, Erich Staudegger, Manfred Kriechbaum, Robert I. Lehrer, Alan J. Waring, Karl Lohner, Susanne Gangl, Bernd Mayer, Gottfried Köhler, J. Shobini, Z. Guttenberg, B. Lortz, B. Hu, E. Sackmann, N. M. Kozlova, L. M. Lukyanenko, A. N. Antonovich, E. I. Slobozhanina, Andrey V. Krylov, Yuri N. Antonenko, Elena A. Kotova, Alexander A. Yaroslavov, Subhendu Ghosh, Amal K. Bera, Sudipto Das, Eva Urbánková, Masood Jelokhani-Niaraki, Karl Freeman, Petr Jezek, P. B. Usmanov, A. Ongarbaev, A. K. Tonkikh, Peter Pohl, Sapar M. Saparov, P. Harikumar, J. P. Reeves, S. Rao, S. K. Sikdar, A. S. Ghatpande, C. Corsso, A. C. Campos de Carvalho, W. A. Varanda, C. ElHamel, E. Dé, N. Saint, G. Molle, Anurae Varshney, M. K. Mathew, E. Loots, E. Y. Isacoff, Michiki Kasai, Naohiro Yamaguchi, Paramita Ghosh, Joseph Tigyi, Gabor Tigyi, Karoly Liliom, Ricardo Miledi, Maja R. Djurisic, Pavle R. Andjus, Indira H. Shrivastava, M. S. P. Sansom, C. Barrias, P. F. Oliveira, A. C. Mauricio, A. M. Rebelo da Costa, I. A. Lopes, S. V. Fedorovich, V. S. Chubanov, M. V. Sholukh, S. V. Konev, N. Fedirko, V. Manko, M. Klevets, N. Shvinka, B. S. Prabhananda, Mamata H. Kombrabail, S. Aravamudhan, Berenice Venegas-Cotero, Ivan Ortega Blake, Zhi-hong Zhang, Xiao-jian Hu, Han-qing Zhou, Wei-ying Cheng, Hang-fang Feng, L. O. Dubitsky, L. S. Vovkanvch, I. A. Zalyvsky, E. Savio-Galimberti, P. Bonazzola, J. E. Ponce-Homos, Mario Parisi, Claudia Capurro, Roxana Toriano, Laxma G. Ready, Larry R. Jones, David D. Thomas, B. A. Tashmukhamedov, B. T. Sagdullaev, D. Heitzmann, R. Warth, M. Bleich, R. Greger, K. T. G. Ferreira, H. G. Ferreira, Orna Zagoory, Essa Alfahel, Abraham H. Parola, Zvi Priel, H. Hama-Inaba, R. Wang, K. Choi, T. Nakajima, K. Haginoya, M. Mori, H. Ohyama, O. Yukawa, I. Hayata, Nanda B. Joshi, Sridhar K. Kannurpatti, Preeti G. Joshi, Mau Sinha, Xun Shen, Tianhui Hu, Ling Bei, Menno L. W. Knetsch, Nicole Schäfers, John Sandblom, Juris Galvanovskis, Roxana Pologea-Moraru, Eugenia Kovacs, Alexandra Dinu, S. H. Sanghvi, V. Jazbinšek, G. Thiel, W. Müller, G. Wübeller, Z. Tronteli, Leš Fajmut, Marko Marhl, Milan Brumen, I. D. Volotovski, S. G. Sokolovski, M. R. Knight, Alexei N. Vasil’ev, Alexander V. Chalyi, P. Sharma, P. J. Steinbach, M. Sharma, N. D. Amin, J. Barchir, R. W. Albers, H. C. Pant, M. Balasubramanyam, M. Condrescu, J. P. Gardner, Shamci Monajembashi, Gotz Pilarczyk, K. O. Greulich, F. M. El-Refaei, M. M. Talaat, A. I. El-Awadi, F. M. Ali, Ivan Tahradník, Jana Pavelková, Alexandra Zahradniková, Boris S. Zhorov, Vettai S. Ananthanaravanan, M. Ch. Michailov, E. Neu, W. Seidenbusch, E. Gornik, D. Martin, U. Welscher, D. G. Weiss, B. R. Pattnaik, A. Jellali, V. Forster, D. Hicks, J. Sahel, H. Dreyfus, S. Picaud, Hong-Wei Wang, Sen-fang Sui, Pradeep K. Luther, John Barry, Ed Morris, John Squire, C. Sivakama Sundari, D. Balasubramanian, K. Veluraia, T. Hema Thanka Christlet, M. Xavier Suresh, V. Laretta-Garde, Dubravka Krilov, Nataša Stojanović, Janko N. Herak, Ravi Jasuja, Maria Ivanova, Rossen Mirchev, Frank A. Ferrone, David Stopar, Ruud B. Spruijt, Cor J. A. M. Wolfs, Marcus A. Hemminga, G. Arcovito, M. De Spirito, Rajendra K. Agrawal, Amy B. Heagle, Pawel Penczek, Robert Grassucci, Joachim Frank, Manjuli R. Sharma, Loice H. Jeyakumar, Sidney Fleischer, Terence Wagenknecht, Carlo Knupp, Peter M. G. Munro, Eric Ezra, John M. Squire, Koji Ichihara, Hidefumi Kitazawa, Yusuke Iguchi, Tomohiko J. Itoh, Greta Pifat, Marina Kveder, Slavko Pečar, Milan Schara, Deepak Nair, Kavita Singh, Kanury V. S. Rao, Kanwaljeet Kaur, Deepti Jain, B. Sundaravadivel, Manisha Goel, D. M. Salunke, E. I. Kovalenko, G. N. Semenkova, S. N. Cherenkevich, T. Lakshmanan, D. Sriram, S. Srinivasan, D. Loganathan, T. S. Ramalingam, J. A. Lebrón, P. J. Bjorkman, A. K. Singh, T. N. Gayatri, Ernesto R. Caffarena, J. Raul Grigera, Paulo M. Bisch, V. Kiessling, P. Fromherz, K. N. Rao, S. M. Gaikwad, M. I. Khan, C. G. Suresh, P. Kaliannan, M. Elanthiraiyan, K. Chadha, J. Payne, J. L. Ambrus, M. P. N. Nair, Madhavan P. N. Nair, S. Mahajan, K. C. Chadha, R. Hewitt, S. A. Schwartz, J. Bourguignon, M. Faure, C. Cohen-Addad, M. Neuburger, R. Ober, L. Sieker, D. Macherel, R. Douce, D. S. Gurumurthy, S. Velmurugan, Z. Lobo, Ratna S. Phadke, Prashant Desai, I. M. Guseinova, S. Yu. Suleimanov, I. S. Zulfugarov, S. N. Novruzova, J. A. Aliev, M. A. Ismayilov, T. V. Savchenko, D. R. Alieva, Petr Ilík, Roman Kouřil, Hana Bartošková, Jan Nauš, Jvoti U. Gaikwad, Sarah Thomas, P. B. Vidyasagar, G. Garab, I. Simidjiev, S. Rajagopal, Zs. Várkonyi, S. Stoylova, Z. Cseh, E. Papp, L. Mustárdy, A. Holzenburg, R. Bruder, U. K. Genick, T. T. Woo, D. P. Millar, K. Gerwert, E. D. Getzoff, Tamás Jávorfí, Győző Garab, K. Razi Naqvi, Md. Kalimullah, Jyoti Gaikwad, Manoj Semwal, Roman Kouril, Petr Ilik, Man Naus, István Pomozi, Gábor Horváth, Rüdiger Wehner, Gary D. Bernard, Ana Damjanović, Thorsten Ritz, Klaus Schulten, Wang Jushuo, Shan Jixiu, Gong Yandao, Kuang Tingyun, Zhao Nanming, Arvi Freiberg, Kõu Timpmann, Rein Ruus, Neal W. Woodbury, E. V. Nemtseva, N. S. Kudryasheva, A. G. Sizykh, V. N. Shikhov, T. V. Nesterenko, A. A. Tikhomirov, Giorgio Forti, Giovanni Finazzi, Alberto Furia, Romina Paola Barbagallo, S. Iskenderova, R. Agalarov, R. Gasanov, Miyashita Osamu, G. O. Nobuhiro, R. K. Soni, M. Ramrakhiani, Hiromasa Yagi, Kacko Tozawa, Nobuaki Sekino, Tomoyuki Iwabuchi, Masasuke Yoshida, Hideo Akutsu, A. V. Avetisyan, A. D. Kaulen, V. P. Skulachev, B. A. Feniouk, Cécile Breyton, Werner Kühlbrandt, Maria Assarsson, Astrid Gräslund, G. Horváth, B. Libisch, Z. Gombos, N. V. Budagovskaya, N. Kudryasheva, Erisa Harada, Yuki Fukuoka, Tomoaki Ohmura, Arima Fukunishi, Gota Kawai, Kimitsuna Watanabe, Jure Derganc, Bojan Božič, Saša Svetina, Boštjan Žekš, J. F. Y. Hoh, Z. B. Li, G. H. Rossmanith, E. L. de Beer, B. W. Treijtel, P. L. T. M. Frederix, T. Blangè, S. Hénon, F. Galtet, V. Laurent, E. Planus, D. Isabey, L. S. Rath, P. K. Dash, M. K. Raval, C. Ramakrishnan, R. Balaram, Milan Randic, Subhash C. Basak, Marjan Vracko, Ashesh Nandy, Dragan Amic, Drago Beslo, Sonja Nikolic, Nenad Trinajstic, J. Walahaw, Marc F. J. Lensink, Boojala V. B. Reddy, Ilya N. Shindylov, Philip E. Bourne, M. C. Donnamaria, J. de Xammar Oro, J. R. Grigera, Monica Neagu, Adrian Neagu, Matej Praprotnik, Dušanka Janežič, Pekka Mark, Lennart Nilsson, L. La Fata, Laurent E. Dardenne, Araken S. Werneck, Marçal de O. Neto, N. Kannan, S. Vishveshwara, K. Veluraja, Gregory D. Grunwald, Alexandra T. Balaban, Kanika Basak, Brian D. Gute, Denise Mills, David Opitz, Krishnan Balasubramanian, G. I. Mihalas, Diana Lungeanu, G. Macovievici, Raluca Gruia, C. Cortez-Maghelly, B. Dalcin, E. P. Passos, S. Blesic, M. Ljubisavljevic, S. Milosevic, D. J. Stratimirovic, Nandita Bachhawat, Shekhar C. Mande, A. Nandy, Ayumu Saito, Koichi Nishigaki, Mohammed Naimuddin, Takatsugu Hirokawa, Mitsuo Ono, Hirotomo Takaesu, M. I. El Gohary, Abdalla S. Ahmed, A. M. Eissa, Hiroshi Nakashima, G. P. S. Raghava, N. Kurgalvuk, O. Goryn, Bernard S. Gerstman, E. V. Gritsenko, N. N. Remmel, O. M. Maznyak, V. A. Kratasyuk, E. N. Esimbekova, D. Tchitchkan, S. Koulchitsky, A. Tikhonov, A. German, Y. Pesotskaya, S. Pashkevich, S. Pletnev, V. Kulchitsky, Umamaheswar Duvvuri, Sridhar Charagundla, Rahim Rizi, John S. Leigh, Ravinder Reddy, Mahesh Kumar, O. Coshic, P. K. Julka, O. K. Rath, NR. Jagannathan, Karina Roxana Iliescu, Maria Sajin, Nicolcta Moisoi, Ileana Petcu, A. I. Kuzmenko, R. P. Morozova, I. A. Nikolenko, G. V. Donchenko, M. K. Rahman, M. M. Ahmed, Takehiro Watanabe, Y. Rubin, H. Gilboa, R. Sharony, R. Ammar, G. Uretzky, M. Khubchandani, H. N. Mallick, V. Mohan Kumar, Arijitt Borthakur, Erik M. Shapiro, M. Gulnaz Begum, Mahaveer N. Degaonkar, S. Govindasamy, Ivan Dimitrov, T. A. Kumosani, W. Bild, I. Stefanescu, G. Titescu, R. Iliescu, C. Lupusoru, V. Nastasa, I. Haulica, Gopal Khetawat, N. Faraday, M. Nealen, S. Noga, P. F. Bray, T. V. Ananieva, E. A. Lycholat, MV. Kosevich, S. G. Stepanyan, S. V. Antonyuk, R. Khachatryan, H. Arakelian, A. Kumar, S. Ayrapetyan, V. Mkheyan, S. Agadjanyan, A. Khachatryan, S. S. Rajan, V. Kabaleeswaran, Geetha Gopalakrishnan, T. R. Govindachari, Meera Ramrakhiani, Phillip Lowe, Andrew Badley, David C. Cullen, H. Hermel, W. Schmahl, H. Möhwald, Nirmalya Majumdar, Joydip Das, András Dér, Loránd Kelemen, László Oroszi, András Hámori, Jeremy J. Ramsden, Pál Ormos, D. Savitri, Chanchal K. Mitra, Toshio Yanagida, Seiji Esaki, Yuji Kimura, Tomoyuki Nishida, Yosiyuki Sowa, M. Radu, V. K. Koltover, Ya. I. Estrin, L. A. Kasumova, V. P. Bubnov, E. E. Laukhina, Rajiv Dotta, M. Degaonkar, P. Raghunathan, Rama Jayasundar, Pavel Novák, Milan Marko, Ivan Zahradník, Hiroaki Hirata, Hidetake Miyata, J. Balaji, P. Sengupta, S. Maiti, M. Gonsalves, A. L. Barker, J. V. Macpherson, D. O’Hare, C. P. Winlove, P. R. Unwin, R. Phillip, S. Banerjee, G. Ravindra Kumar, K. Nagayaka, R. Danev, S. Sugitani, K. Murata, Michael Gősch, H. Blom, P. Thyberg, Z. Földes-Papp, G. Björk, J. Holm, T. Heino, Masashi Yokochi, Fuyuhiko Inagaki, Masami Kusunoki, E. K. Matthews, J. Pines, Yu. P. Chukova, Vitaly K. Koltover, Geetanjali Bansal, Uma Singh, M. P. Bansal, Kotoko Nakata, Tastuya Nakano, Tsuguchika Kaminuma, B. P. S. Kang, U. Singh, Bonn Kirn, Neja Potocnik, Vito Stare, Latal Shukla, V. Natarajan, T. P. A. Devasagayam, M. D. Sastry, P. C. Kesavan, R. Sayfutdinov, V. V. Adamovich, D. Yu. Rogozin, A. G. Degermendzhy, C. L. Khetrapal, G. A. Nagana Gowda, Kedar Nath Ghimire, Ishida Masaru, H. Fujita, S. Ishiwata, Y. Kishimoto, S. Kawahara, M. Suzuki, H. Mori, M. Mishina, Y. Kirino, H. Ohshima, A. S. Dukhin, V. N. Shilov, P. J. Goetz, and R. K. Mishra

Subjects
0303 health sciences, biology, General Medicine, 010402 general chemistry, 01 natural sciences, Horseradish peroxidase, General Biochemistry, Genetics and Molecular Biology, 0104 chemical sciences, 03 medical and health sciences, Biochemistry, Manganese porphyrin, biology.protein, Enzyme reconstitution, General Agricultural and Biological Sciences, 030304 developmental biology
Published
1999
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2. Fragment Reconstitution of a Small Protein: Folding Energetics of the Reconstituted Immunoglobulin Binding Domain B1 of Streptococcal Protein G

Author

Shinya Honda, Eisuke Munekata, H. Uedaira, and Naohiro Kobayashi

Subjects
Models, Molecular, Protein Folding, Circular dichroism, Protein Conformation, Globular protein, Biochemistry, Protein Structure, Secondary, Protein structure, Bacterial Proteins, Denaturation (biochemistry), chemistry.chemical_classification, Antigens, Bacterial, Calorimetry, Differential Scanning, biology, Chemistry, Circular Dichroism, Peptide Fragments, Folding (chemistry), Kinetics, Crystallography, Models, Chemical, Immunoglobulin G, biology.protein, Thermodynamics, Protein folding, Binding Sites, Antibody, Protein G, Immunoglobulin binding
Abstract

To elucidate early stages in protein folding, we have adopted a fragment reconstitution method for small proteins. This approach is expected to provide nuclei for protein folding and to allow us to investigate folding mechanisms. In previous work [Kobayashi, N., et al. (1995) FEBS Lett. 366, 99-103.] we demonstrated the association of two complementary fragments, derived from the immunoglobulin G-binding domain B1 of streptococcal Protein G, and showed the structural similarity between the reconstituted domain and the uncleaved wild-type domain. In this work we have further characterized the reconstituted domain as well as the uncleaved domain thermodynamically by means of differential scanning calorimetry (DSC) and circular dichroism (CD) measurements. Although composed of short peptide fragments not linked by covalent bonds, the reconstituted domain showed a typical folding/unfolding curve in both DSC and CD melting measurements and behaved like a globular protein. The domain was not very stable, and the small value of the Gibbs free energy corresponded to the class of the weakest protein-protein binding systems. The denaturation temperature of 0. 78 mM solution was 313 K at pH 5.9 as measured by DSC, which was more than 40 degrees lower than the uncleaved domain. This apparent instability was primarily caused by entropic disadvantage attributed to a bimolecular reaction. The temperature dependence of the enthalpy change from the folded to the unfolded state was almost identical for the reconstituted domain and the uncleaved one. This indicates that most of the noncovalent intramolecular interactions stabilizing the native structure, such as hydrogen bonding and hydrophobic interactions, are regenerated in the reconstituted domain. By comparing the equilibrium constants of the reconstituted and uncleaved domains, we determined the effective concentration to be approximately 6 M at 298 K. Structure-based estimation of the thermodynamic properties from the values of accessible surface areas showed that approximately 35% of the total heat capacity change and approximately 25% of the total enthalpy change can be attributed to the interchain interaction at 298 K. Furthermore, the folding/unfolding equilibrium of beta-hairpin structure of the fragment 41-56 alone was also characterized. These analyses allow us to envision the microdomain folding mechanism of the Protein G B1 domain, in which segment 41-56 first forms a stable beta-hairpin structure and then collides with segment 1-40, followed by spontaneous folding of the whole molecule.

Published
1999
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3. Thermal denaturation of photosynthetic membrane proteins from Rhodobacter sphaeroides

Author

Takayuki Odahara, Jun Miyake, Shinya Honda, H. Uedaira, and Miyuki Ishimura

Subjects
Circular dichroism, biology, Chemistry, Analytical chemistry, Condensed Matter Physics, biology.organism_classification, Absorbance, Rhodobacter sphaeroides, Differential scanning calorimetry, Denaturation (biochemistry), Photosynthetic membrane, Physical and Theoretical Chemistry, Rhodospirillales, Instrumentation, Rhodospirillaceae
Abstract

The thermal stability of detergent-solubilized reaction centers (RC) and light-harvesting B800–850 complex from Rhodobacter sphaeroides was studied by the temperature-scanning (T-scan) method in the absorbance mode and circular dichroism (CD), and by DSC. The denaturation temperatures of RC solubilized with n -octyl β- d -glucoside (OG) and lauryl-dimethylamine N -oxide (LDAO) obtained by the T-scan method did not depend on wavelengths or the methods of measurement. The denaturation temperature T d of B800–850 complex was higher than that of RC in all measurements. The values of T d measured at various wavelengths for RC in OG was about 10 K higher than those in LDAO. The value of T d of B800–850 complex in OG obtained by T-scan CD at 290 nm was about 7 K higher than that in LDAO. Compared with LDAO, OG has a stabilizing effect on both RC and B800–850 complex against heat denaturation.

Published
1995
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4. Volume and compressibility changes on mixing aqueous solutions of the amino acid and poly(ethylene glycol)

Author

K. Sasahara and H. Uedaira

Subjects
Alanine, chemistry.chemical_classification, Molality, Chromatography, Polymers and Plastics, Chemistry, technology, industry, and agriculture, Thermodynamics, Phenylalanine, Amino acid, Hydrophobic effect, chemistry.chemical_compound, Colloid and Surface Chemistry, Materials Chemistry, Compressibility, Side chain, Physical and Theoretical Chemistry, Ethylene glycol
Abstract

The volume and compressibility changes on mixing aqueous solutions of the amino acid and poly(ethylene glycol) were measured with a vibration densimeter and a sing-around velocimeter at 298.15 K. For the system of alanine-PEG-H2O, the additivity rule for the mean apparent molal volume and compressibility at infinite dilution held, and the excess volume and compressibility changes on mixing were obtained. For the system of glycine-PEG-H2O, the additivity rule for the mean apparent molal compressibility at infinite dilution did not hold. While the mean apparent molal volume and compressibility changes were negative and positive for the systems of another amino acid-PEG-H2O, respectively, where amino acids were valine, isoleucine, leucine, phenylalanine, and tryptophan. These results suggest that glycine and alanine are excluded from the hydration layer around PEG chain and the amino acids with a larger side chain than alanine are bound to the PEG chain due to the hydrophobic interaction. The hydration number per monomer around PEG chain was estimated to be 3.9.

Published
1994
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5. Solubility of amino acids in aqueous poly (ethylene glycol) solutions

Author

K. Sasahara and H. Uedaira

Subjects
chemistry.chemical_classification, Aqueous solution, Polymers and Plastics, technology, industry, and agriculture, Amino acid, Hydrophobic effect, chemistry.chemical_compound, Colloid and Surface Chemistry, chemistry, Polymer chemistry, PEG ratio, Materials Chemistry, Side chain, Organic chemistry, Physical and Theoretical Chemistry, Solubility, Ethylene glycol, Equilibrium constant
Abstract

The solubilities of amino acids have been measured in water and aqueous poly(ethylene glycol) (PEG) solutions as a function of temperature and PEG concentration. The free energies of transfer from water to aqueous PEG solutions forl-alanine,l-valine,l-isoleucine andl-leucine were positive, while those forl-phenylalanine andl-tryptophan were negative. The corresponding enthalpies of transfer were almost zero for all amino acids. The equilibrium constants of the binding of amino acids to PEG chain were estimated from the solubility data. Amino acids with larger hydrophobicity are bound more strongly to the PEG chain due to the hydrophobic interaction between the methylene groups of PEG and the side chain of amino acid. The equilibrium constants showed a correlation with the dynamic hydration number (nDHN) which expresses the hydration properties of amino acids in aqueous solution.

Published
1993
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6. Thermal stability of the DNA-binding domain of the Myb oncoprotein

Author

Kazuhiro Ogata, Yoshifumi Nishimura, Shunsuke Ishii, Hisayuki Morii, Takashi Yasukawa, H. Uedaira, and Akinori Sarai

Subjects
Protein Denaturation, Circular dichroism, Base Sequence, Calorimetry, Differential Scanning, Sequence Homology, Amino Acid, Protein Conformation, Circular Dichroism, Transition temperature, Molecular Sequence Data, DNA, DNA-binding domain, Biology, Biochemistry, DNA-Binding Proteins, Proto-Oncogene Proteins c-myb, Crystallography, Differential scanning calorimetry, Protein structure, Tandem repeat, Proto-Oncogene Proteins, Thermodynamics, Intermediate state, Denaturation (biochemistry), Amino Acid Sequence
Abstract

The DNA-binding domain of the c-myb protooncogene product consists of three homologous tandem repeats of 51-52 amino acids (denoted as R1, R2, and R3 from the N-terminal side). In order to analyze conformational and thermodynamic characteristics of the homologous repeats, we have examined the DNA-binding domain by circular dichroism (CD) and differential scanning calorimetry (DSC). The CD spectra for the three individual repeats are significantly different in the fine profiles, indicating subtle differences in their conformations. The melting analyses for the fragments show that the thermal stability of each fragment is different from one another, with the following order of stability: R1(Tm = 61 degrees C) approximately greater than R3(57 degrees C) >> R2(43 degrees C), where R2 is much less stable than the other repeats. The denaturing process for the whole DNA-binding domain, measured by DSC, is characterized by a very broad transition ranging from 30 to 80 degrees C. The denaturation curve can be fit well by a three-state transition with one intermediate state. The transition temperature for the native-to-intermediate transition coincides with the melting temperature of R2, indicating that the intermediate state corresponds to the unfolding of unstable R2. The CD spectrum of the whole domain is almost identical to the sum of the individual spectra. Thus, these results suggest that the individual repeats in the whole DNA-binding domain behave independently in terms of conformation and stability. The addition of DNA to the DNA-binding fragment drastically changed the melting profile, in which the broad transition curve was replaced by a sharp peak at 58 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)

Published
1993
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7. Thermostability of Rhodopseudomonas viridis and Rhodospirillum rubrum chromatophores reflecting physiological conditions

Author

Ayako Ooishi, Jun Miyake, Noriyuki Ishii, Takayuki Odahara, Masayuki Hara, Shinya Honda, and H. Uedaira

Subjects
Circular dichroism, Absorption spectroscopy, Photosynthetic Reaction Center Complex Proteins, Biophysics, Photochemistry, Photosynthesis, Rhodospirillum rubrum, Biochemistry, Differential scanning calorimetry, Photosynthetic bacterium, Photoreaction unit, Thermostability, Protein Unfolding, Chromatophore, biology, Calorimetry, Differential Scanning, Protein Stability, Circular Dichroism, Temperature, Cholic Acids, Cell Biology, Bacterial Chromatophores, biology.organism_classification, Microscopy, Electron, Rhodopseudomonas, Membrane, Spectrophotometry
Abstract

Relationships between growth conditions and thermostability were examined for photosynthetic inner membranes (chromatophores) from Rhodopseudomonas viridis and Rhodospirillum rubrum of which morphology, lipid composition, and protein/lipid rate are rather mutually different. Signals observed by differential scanning calorimetry of the chromatophores were correlated with thermal state transitions of the membrane components by reference to temperature dependencies of circular dichroism and absorption spectra of the purified supramolecule comprising a photoreaction center and surrounding light-harvesting pigment–protein complexes that are the prominent proteins in both membranes. The differential scanning calorimetry curves of those chromatophores exhibited different dependencies on growth stages and environmental temperatures. The obtained result appeared to reflect the differences in the protein/lipid rate and protein–lipid specificity between the two chromatophores.

Published
2010

8. Characteristics of an adiabatic differential scanning microcalorimeter

Author

S. Kidokoro and H. Uedaira

Subjects
Chemistry, Time constant, Analytical chemistry, Thermodynamics, Condensed Matter Physics, Heat capacity, Calorimeter, Data analysis, Calibration, Physical and Theoretical Chemistry, Adiabatic process, Instrumentation, Electrical conductor, Differential (mathematics)
Abstract

An on-line system was designed for the acquisition and analysis of data from the differential adiabatic scanning microcalorimeter DASM-1M. The characteristics of the calorimeter, temperature dependence of the heating rates, calibration of the heat capacity and time constants of the apparatus at various heating rates were obtained. The heat capacity data of lysozyme measured with the DASM-1M were compared with those using a conductive type DSC instrument, the micro-DSC.

Published
1991
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9. Fibrous Support Module Composed of Braided Poly(Vinyl Alcohol) Superfine Fibers

Author

Shinya Honda, Hisao Ichijo, Michiaki Sagesaka, Tetsuro Suehiro, Noboru Aisaka, Aizo Yamauchi, Jun'ichi Nagasawa, and H. Uedaira

Subjects
chemistry.chemical_compound, Hydrolysis, Vinyl alcohol, Sucrose, History and Philosophy of Science, chemistry, General Neuroscience, Organic chemistry, Fermentation, General Biochemistry, Genetics and Molecular Biology
Published
1990
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10. Thermal transition of a mutated dihydrofolate reductase

Author

Shinichi Ohashi, Shinya Honda, H. Uedaira, Masahiro Iwakura, and Shun-ichi Kidokoro

Subjects
biology, Chemistry, Thermal transition, Mutant, Condensed Matter Physics, Mole fraction, law.invention, Biochemistry, law, parasitic diseases, Dihydrofolate reductase, biology.protein, Recombinant DNA, Physical and Theoretical Chemistry, Amino acid residue, Instrumentation
Abstract

A mutated dihydrofolate reductase(DHFR), in which Cys 152 of wild DHFR was replaced by Glu and three amino acid residues(Ile-Gln-Ile) were added at C terminal. was obtained by a recombinant DNA method. The thermal transition of the mutant was measured by CD and DSC at pH 7.0 and 7.7 and compared with that of wild DHFR. Analysis of the DSC data revealed that the thermal transition was the three-state one and the thermodynamic functions and mole fractions of native, intermediate and denatured states were calculated.

Published
1990
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12. Identification of a key amino acid residue of Streptomyces phospholipase D for thermostability by in vivo DNA shuffling

Author

Yoshiko Uesugi, Yuko Kawasaki, Hiroyuki Aoki, H. Uedaira, Tomofumi Negishi, Takafumi Mukaihara, Koichi Mori, Tadashi Hatanaka, Hiroko Nishikido, Michiko Kodama, and Masaki Iwabuchi

Subjects
DNA, Bacterial, Models, Molecular, Protein Denaturation, Recombinant Fusion Proteins, Mutant, Molecular Sequence Data, Restriction Mapping, Biophysics, Biology, Biochemistry, Streptomyces, Restriction map, Enzyme Stability, Phospholipase D, Amino Acid Sequence, Thermolabile, Molecular Biology, Peptide sequence, Thermostability, DNA Primers, chemistry.chemical_classification, Base Sequence, Sequence Homology, Amino Acid, Circular Dichroism, biology.organism_classification, Molecular biology, DNA shuffling, Amino acid, chemistry, Plasmids
Abstract

To isolate thermostability-related amino acid residues of Streptomyces phospholipase D (PLD), we constructed a chimeral genes library between two highly homologous plds, which exhibited different thermostabilities, by an in vivo DNA shuffling method using Escherichia coli that has a mutation of a single-stranded DNA-binding protein gene. To confirm the location of the recombination site, we carried out the restriction mapping of 68 chimeral pld genes. The recombination sites were widely dispersed over the entire pld sequence. Moreover, we examined six chimeral PLDs by comparing their thermostabilities with those of parental PLDs. To identify a thermostability-related amino acid residue, we investigated the thermostability of chimera C that was the most thermolabile among the six chimeras. We identified the thermostability-related factor Gly-188, which is located in the alpha-7 helix of PLD from Streptomyces septatus TH-2 (TH-2PLD). TH-2PLD mutants, in which Gly-188 was substituted with Phe, Val or Trp, exhibited higher thermostabilities than that of the parental PLD. Gly-188 substituted with the Phe mutant, which was the most stable among the mutants, showed an enzyme activity almost the same as that of TH-2PLD as determine by kinetic analysis.

Published
2004

13. Role of hydration of polyhydroxy compounds in biological systems

Author

H, Uedaira

Subjects
Solutions, Hemoglobins, Protein Denaturation, Magnetic Resonance Spectroscopy, Polymers, Alcohols, Carbohydrates, Temperature, Animals, Asparaginase, Water, Collagen
Abstract

The spin-lattice relaxation times, T1, of H2(17)O have been measured for aqueous solutions of 9 polyols as a function of the concentration at 25 degrees C. The dynamic hydration number, nDHN, for polyols were obtained. The values of nDHN increased with an increase in the number of OH groups and depended on the conformation of isomers. The value of nDHN for inositol was the largest. This means that the thermal motion of water molecules around inositol is most inhibited among the polyols studied. The increment of thermal stability of proteins by polyols and sugars, the equilibrium distribution coefficients of polyols and sugars in the denatured hemoglobin solution, and the effect of sugars on the osmotic flow of water were expressed by linear relation of nDHN. On the bases of these relations, a systematic treatment for the effect of hydration of polyols and sugars on these phenomena is discussed.

Published
2001

14. Folding energetics of a multidomain protein, flagellin

Author

S, Honda, H, Uedaira, F, Vonderviszt, S, Kidokoro, and K, Namba

Subjects
Salmonella typhimurium, Protein Denaturation, Protein Folding, Calorimetry, Differential Scanning, Models, Chemical, Ultraviolet Rays, Circular Dichroism, Temperature, Thermodynamics, Peptide Fragments, Flagellin
Abstract

Thermodynamic investigations of flagellin from Salmonella typhimurium and its proteolytic fragments were conducted by differential scanning calorimetry (DSC) and circular dichroism (CD) melting measurements. A new method of analysis for a multi-state transition based on our original theoretical treatment of thermodynamic equations has been developed to analyze those data. The analysis of DSC curves confirmed the three thermodynamic domains of flagellin. The thermodynamic parameters of each domain were revised from those previously reported and the new values of the parameters have a good correlation to the apparent molecular masses of the morphological domains. CD melting measurements at far and near-UV wavelengths showed sequential unfolding of the domains. Therefore, we could reasonably assign the thermodynamically identified domains to the morphological domains. Further analysis of both DSC and CD data provided insights into the folding energetics of the multidomain structure of flagellin. An inner domain (Df1) of flagellin in the filament unfolds through a relatively broad transition, while the two outer domains unfold cooperatively and show sharp transitions. This indicates that the interdomain interactions between Df1 and D2 has different characteristics from the apparently more intimate interactions between D2 and D3. These characteristics suggest that flagellin is organized with relatively flexible domains and rigid domains, which appears to be responsible for the well-regulated assembly mechanism of the bacterial flagellar filament.

Published
1999

15. Mechanism of self-association and filament capping by flagellar HAP2

Author

F, Vonderviszt, K, Imada, Y, Furukawa, H, Uedaira, H, Taniguchi, and K, Namba

Subjects
Magnetic Resonance Spectroscopy, Bacterial Proteins, Sequence Homology, Amino Acid, Flagella, Protein Conformation, Molecular Sequence Data, Temperature, Amino Acid Sequence, Peptide Fragments, Protein Structure, Secondary, Flagellin
Abstract

HAP2 forms a capping structure, which binds very tightly to the distal end of flagellar filaments and still allows insertion of flagellin subunits below the cap by an unknown mechanism. Terminal regions of HAP2 from Salmonella typhimurium were found to be quickly degraded by various proteases, indicating that HAP2 also possesses disordered terminal regions like other axial proteins of bacterial flagellum. Removal of these portions by trypsin results in a fragment of 40 kDa (HP40), which lacks 42 NH2-terminal and 51 COOH-terminal residues. HAP2 in solution readily associates into a decameric structure without any significant population of intermediate oligomeric forms. The HP40 fragments, however, do not form decamers, while they can assemble into pentamers, as revealed by chemical cross-linking and analytical ultracentrifugation. Decameric HAP2 also dissociates into pentamers and smaller oligomers upon a heat induced conformational transition around 36 degreesC. While the highly mobile terminal regions are immobilized in decameric HAP2 complexes, they are still largely disordered in the pentameric state. These results demonstrate that the intersubunit interactions within the pentamers are mainly through the HP40 portions, whereas the terminal regions are responsible for association of pentamers into decameric complexes. Several observations indicate that HAP2 performs its capping function as a pentamer. We suggest that binding of the pentameric HAP2 cap to the filament is mediated by the highly flexible terminal regions. Indeed, HP40 fragments are unable to cap the end of filaments, while removal of about 30 residues from both terminal regions of HAP2 results in a highly reduced capping ability. A model is presented to explain the molecular mechanism of capping, in which conformational entropy in the disordered terminal regions moderates the otherwise too tight HAP2-filament interactions to allow insertion of flagellin subunits below the cap.

Published
1999

17. Proton NMR spectroscopic studies of serum as an aid to perioperative cellular metabolic monitoring

Author

T, Tatara, J, Noguchi, K, Fukushima, Y, Ishihara, S, Ohkochi, and H, Uedaira

Subjects
Adult, Blood Glucose, Male, Alanine, Magnetic Resonance Spectroscopy, Esophageal Neoplasms, Rectal Neoplasms, Fatty Acids, Nonesterified, Reference Values, Stomach Neoplasms, Monitoring, Intraoperative, Neoplasms, Lactates, Humans, Blood Chemical Analysis, Aged, Glycoproteins
Abstract

Perioperative concentration changes of cellular metabolites in serum were studied by proton NMR spectroscopy in four cancer patients who underwent tumorectomies under general anesthesia. In proton NMR spectra of serum, the resonances assignable to fatty acid in lipoprotein, lactate, alanine, glucose, glycoprotein and other metabolites were observed. The concentrations of fatty acid and alanine did not show significant changes during the operations compared with those in healthy volunteers. The concentrations of lactate, glucose and glycoprotein increased during the operations above the concentration ranges in the control subjects. The time-course of concentration change for lactate, glucose and glycoprotein was roughly classified into two patterns: i) the maximums of lactate and glucose concentration were observed in the latter halves or at the ends of the operations; ii) the maximums of glycoprotein concentrations were observed three hours after the incision, regardless of the operative time. The results showed cellular metabolic changes became larger as the operations proceeded responding to surgical stress. Prompt cellular metabolic monitoring is indispensable for the screening of cellular metabolic disorders caused by excessive surgical stress and proton NMR spectroscopy can be a new tool for monitoring perioperative cellular metabolism.

Published
1995

19. 1H-NMR spectroscopic analysis of human urine: periodic variation of trimethylamine oxide excretion

Author

Y, Hirama, N, Shinriki, T, Fujino, and H, Uedaira

Subjects
Adult, Methylamines, Periodicity, Magnetic Resonance Spectroscopy, Creatinine, Humans, Female, Histidine, Syndrome, Hydrogen-Ion Concentration, Urine, Oxidants, Hydrogen
Abstract

We used 1H-NMR to study the constituents of the urine from a female volunteer who had an unidentified complaint syndrome (chief complaints: discomfort of scapular region, abdominal distention and exhaustion). The pH dependence of the chemical shift of some constituents was investigated for signal assignments, and the intense peak at about 3.3 ppm was assigned to trimethylamine oxide (TMAO). We measured the concentration of the constituents of urine, and TMAO excretion in the urine over a three week time period. The TMAO excretion fluctuated in a cycle of about 2 days. The average excretion determined (3.8 mmole/day) is considerably higher than data of healthy humans that had been previously reported (0.3 to 0.5 mmole/day).

Published
1993

21. Immobilization of Bioactive Substances with PVA Supports

Author

Hisao Ichijo, H. Uedaira, Jun'ichi Nagasawa, Noboru Aisaka, Kunihiro Ichimura, Aizo Yamauchi, and Tetsuro Suehiro

Subjects
Bioactive substance, Materials science, Adsorption rate constant, Nanotechnology
Abstract

A variety of methods and materials for immobilizing biocatalysts have been proposed and tested. All of the different methods or materials has some advantages and disadvantages. No one technique or support seems to have a clear edge over the others. In any case, the technique or support, which can make the most of the advantage and minimize the disadvantage, should be selected.

Published
1991
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30. Effect of the degree of polymerization and etherification on the binding of acridine orange by sodium carboxymethyl cellulose

Author

T. Akimoto, H. Shindate, H. Uedaira, and K. Nishida

Subjects
Polymers and Plastics, Sodium, Acridine orange, technology, industry, and agriculture, chemistry.chemical_element, macromolecular substances, Degree of polymerization, Carboxymethyl cellulose, chemistry.chemical_compound, Colloid and Surface Chemistry, chemistry, Polymerization, Polymer chemistry, Materials Chemistry, medicine, Physical and Theoretical Chemistry, Cellulose, Binding site, medicine.drug, Electrostatic interaction
Abstract

The interaction between sodium carboxymethyl cellulose and acridine orange was studied by spectral method. The effect of the degree of polymerization and etherification on the binding of the dye was discussed. The binding value increases with an increase in the degree of the polymerization. The number of binding sites per unit glucose was larger than the degree of etherification. Therefore, the electrostatic interaction was probably not the predominant factor.

Published
1971
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31. Na+ interacting with gramicidin D. A nuclear magnetic resonance study

Author

H. Monoi and H. Uedaira

Subjects
Larmor precession, Magnetic Resonance Spectroscopy, Chemistry, Relaxation (NMR), Sodium, Analytical chemistry, Biophysics, Gramicidin, Resonance, Biological membrane, Nuclear magnetic resonance spectroscopy, Models, Biological, Ion Channels, chemistry.chemical_compound, Nuclear magnetic resonance, Absorption (chemistry), Mathematics, Line (formation), Research Article
Abstract

23Na nuclei in a milk-white emulsion composed to nonionic surfactant and higher alcohol in saline were characterized by single values of T1 and T2 and a single Larmor frequency. In the presence of small amounts of gramicidin D (Dubos), the relaxations of 23Na were greatly accelerated, and the transverse relaxation was a sum of two decaying exponentials. But only a single T1 was observed; it was roughly equal to the slow T2. The slow T2 accounted for about 40% of the total resonance intensity. The relaxation rates increased linearly with the increase of the gramicidin concentration. The absorption signal consisted of a narrow and a broad line, both centered at the same frequency. The present results suggest that nuclear magnetic resonance spectroscopy is a useful tool for studying the nature of ion-permeable channels of biological membranes, even when the channel has no ionizable groups.

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34. Interaction of dye and polysaccharides

Author

H. Uedaira, K. Nishida, and T. Akimoto

Subjects
chemistry.chemical_classification, Polymers and Plastics, Chemistry, Enthalpy, Polymer, Polysaccharide, Binding constant, chemistry.chemical_compound, Colloid and Surface Chemistry, Amylose, Materials Chemistry, Organic chemistry, Physical chemistry, Physical and Theoretical Chemistry, Entropy (order and disorder)
Abstract

The interactions between amylose, amylodextrine and Benzopurpurine 4 B were studied by spectral and equilibrium dialyses methods. From the binding constant of amylose and amylodextrine, the molar changes in entropy and enthalpy for binding of the dye were calculated. BothΔH° andΔS° were positive. The positive value ofΔS° may be explained by the increase of flexibility of the polymer chain with increasing temperature.

Published
1969
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35. Interaction of dye and synthetic sucrose polymer Ficoll

Author

I. Ishige, S. Yoshida, K. Nishida, and H. Uedaira

Subjects
chemistry.chemical_classification, Chromatography, Sucrose, Polymers and Plastics, Chemistry, Intrinsic viscosity, Enthalpy, Ficoll, Polymer, Viscosity measurement, chemistry.chemical_compound, Colloid and Surface Chemistry, Chemical engineering, Materials Chemistry, Benzopurpurine 4B, sense organs, Physical and Theoretical Chemistry, Entropy (order and disorder)
Abstract

The interaction of Ficoll and Benzopurpurine 4B was studied by spectral method and viscosity measurement. From the binding data the molar changes in entropy and enthalpy, and the number of binding sites on polymer were calculated. Both values of ΔH0 and ΔS0 were positive. The valuen increases with increasing temperature. These results may be explained by the change of the configuration of polymer chain. The intrinsic viscosity reduction in the presence of the dye is due to the formation of dye bridges.

Published
1970
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37. Acoustical investigation of poly(dA).poly(dT), poly[d(A-T)], poly(A).poly(U) and DNA hydration in dilute aqueous solutions

Author

Vitaly Buckin, B. I. Kankiya, A. P. Sarvazyan, and H. Uedaira

Subjects
Chemical Phenomena, Cesium, Biology, Ion, Molar volume, Polydeoxyribonucleotides, Poly dA-dT, Genetics, Magnesium, Ultrasonics, chemistry.chemical_classification, Base Composition, Aqueous solution, Ionic atmosphere, Chemistry, Physical, Osmolar Concentration, Water, Polymer, Solutions, Crystallography, chemistry, Biochemistry, Polynucleotide, Helix, Nucleic Acid Conformation, Poly A-U, Counterion
Abstract

Apparent molar adiabatic compressibilities and apparent molar volumes of poly[d(A-T)].poly[d(A-T)], poly(dA).poly(dT), DNA and poly(A).poly(U) in aqueous solutions were determined at 1 degree C. The change of concentration increment of the ultrasonic velocity upon replacing counter ion Cs+ by the Mg2+ ion was also determined for these polymers. The following conclusions have been made: (1) the hydration of the double helix of poly(dA).poly(dT) is remarkably larger than that of other polynucleotides; (2) the hydration of the AT pair in the B-form DNA is larger than that of the GC pair; (3) the substitution of Cs+ for Mg2+ ions as counter ions results in a decrease of hydration of the system polynucleotide plus Mg2+, and (4) the magnitude of this dehydration depends on the nucleotide sequence; the following rule is true: the lesser is a polynucleotide hydration, the larger dehydration upon changing Cs+ for Mg2+ ions in the ionic atmosphere of polynucleotide.

Published
1989

38. [Water in biological systems (author's transl)]

Author

H, Uedaira

Subjects
Erythrocytes, Time Factors, Body Water, Models, Chemical, Protein Conformation, Muscles, Animals, Thermodynamics, Hydrogen Bonding, Mitochondrial Swelling, Absorption, Mitochondria, Rats
Published
1976

40. [Physical chemistry of aqueous urea solutions]

Author

H, Uedaira

Subjects
Diffusion, Solutions, Chemistry, Chemical Phenomena, Chemistry, Physical, Temperature, Thermodynamics, Urea, Water, Dipeptides, Amino Acids, Calorimetry
Published
1973

41. Thermal stability of free and immobilized glucose oxidase studied by activity assay and calorimetry

Author

Aizo Yamauchi, Hisao Ichijo, H. Uedaira, Tetsuro Suehiro, Jun'ichi Nagasawa, and Noboru Aisaka

Subjects
Thermal denaturation, chemistry.chemical_classification, Chromatography, biology, Immobilized enzyme, Chemistry, Aspergillus niger, Calorimetry, biology.organism_classification, General Biochemistry, Genetics and Molecular Biology, Invertase, Enzyme, biology.protein, Glucose oxidase, Thermal stability, General Agricultural and Biological Sciences
Abstract

In this work, the thermal stability of glucose oxidase in solution and immobilized on SFF was measured by an activity assay and calorimetry. The results from the glucose oxidase on SFF are similar to those of the invertase on SFF, but the T d difference between free and immobilized enzyme is less for glucose oxidase than for invertase

Published
1989
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42. Thermostability of Rhodopseudomonas viridis and Rhodospirillum rubrum chromatophores reflecting physiological conditions.

Author

Odahara T, Ishii N, Ooishi A, Honda S, Uedaira H, Hara M, and Miyake J

Subjects
Bacterial Chromatophores ultrastructure, Calorimetry, Differential Scanning, Cholic Acids chemistry, Circular Dichroism, Microscopy, Electron, Photosynthetic Reaction Center Complex Proteins metabolism, Protein Stability, Protein Unfolding, Rhodopseudomonas growth & development, Rhodospirillum rubrum growth & development, Spectrophotometry, Temperature, Bacterial Chromatophores chemistry, Photosynthetic Reaction Center Complex Proteins chemistry, Rhodopseudomonas chemistry, Rhodospirillum rubrum chemistry
Abstract

Relationships between growth conditions and thermostability were examined for photosynthetic inner membranes (chromatophores) from Rhodopseudomonas viridis and Rhodospirillum rubrum of which morphology, lipid composition, and protein/lipid rate are rather mutually different. Signals observed by differential scanning calorimetry of the chromatophores were correlated with thermal state transitions of the membrane components by reference to temperature dependencies of circular dichroism and absorption spectra of the purified supramolecule comprising a photoreaction center and surrounding light-harvesting pigment-protein complexes that are the prominent proteins in both membranes. The differential scanning calorimetry curves of those chromatophores exhibited different dependencies on growth stages and environmental temperatures. The obtained result appeared to reflect the differences in the protein/lipid rate and protein-lipid specificity between the two chromatophores., (Copyright © 2011 Elsevier B.V. All rights reserved.)

Published
2011
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43. ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions.

Author

Kumar MD, Bava KA, Gromiha MM, Prabakaran P, Kitajima K, Uedaira H, and Sarai A

Subjects
DNA metabolism, DNA-Binding Proteins chemistry, Internet, Mutation, Proteins genetics, Proteins metabolism, RNA metabolism, RNA-Binding Proteins chemistry, User-Computer Interface, DNA chemistry, Databases, Genetic, Proteins chemistry, RNA chemistry, Thermodynamics
Abstract

ProTherm and ProNIT are two thermodynamic databases that contain experimentally determined thermodynamic parameters of protein stability and protein-nucleic acid interactions, respectively. The current versions of both the databases have considerably increased the total number of entries and enhanced search interface with added new fields, improved search, display and sorting options. As on September 2005, ProTherm release 5.0 contains 17,113 entries from 771 proteins, retrieved from 1497 scientific articles (approximately 20% increase in data from the previous version). ProNIT release 2.0 contains 4900 entries from 273 research articles, representing 158 proteins. Both databases can be queried using WWW interfaces. Both quick search and advanced search are provided on this web page to facilitate easy retrieval and display of the data from these databases. ProTherm is freely available online at http://gibk26.bse.kyutech.ac.jp/jouhou/Protherm/protherm.html and ProNIT at http://gibk26.bse.kyutech.ac.jp/jouhou/pronit/pronit.html.

Published
2006
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44. Identification of a key amino acid residue of Streptomyces phospholipase D for thermostability by in vivo DNA shuffling.

Author

Negishi T, Mukaihara T, Mori K, Nishikido H, Kawasaki Y, Aoki H, Kodama M, Uedaira H, Uesugi Y, Iwabuchi M, and Hatanaka T

Subjects
Amino Acid Sequence, Base Sequence, Circular Dichroism, DNA Primers, Enzyme Stability, Models, Molecular, Molecular Sequence Data, Phospholipase D chemistry, Plasmids, Protein Denaturation, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins metabolism, Restriction Mapping, Sequence Homology, Amino Acid, DNA, Bacterial metabolism, Phospholipase D metabolism, Streptomyces enzymology
Abstract

To isolate thermostability-related amino acid residues of Streptomyces phospholipase D (PLD), we constructed a chimeral genes library between two highly homologous plds, which exhibited different thermostabilities, by an in vivo DNA shuffling method using Escherichia coli that has a mutation of a single-stranded DNA-binding protein gene. To confirm the location of the recombination site, we carried out the restriction mapping of 68 chimeral pld genes. The recombination sites were widely dispersed over the entire pld sequence. Moreover, we examined six chimeral PLDs by comparing their thermostabilities with those of parental PLDs. To identify a thermostability-related amino acid residue, we investigated the thermostability of chimera C that was the most thermolabile among the six chimeras. We identified the thermostability-related factor Gly-188, which is located in the alpha-7 helix of PLD from Streptomyces septatus TH-2 (TH-2PLD). TH-2PLD mutants, in which Gly-188 was substituted with Phe, Val or Trp, exhibited higher thermostabilities than that of the parental PLD. Gly-188 substituted with the Phe mutant, which was the most stable among the mutants, showed an enzyme activity almost the same as that of TH-2PLD as determine by kinetic analysis.

Published
2005
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45. ProTherm, version 4.0: thermodynamic database for proteins and mutants.

Author

Bava KA, Gromiha MM, Uedaira H, Kitajima K, and Sarai A

Subjects
Animals, Humans, Internet, Structure-Activity Relationship, Temperature, Thermodynamics, Databases, Protein, Mutation genetics, Proteins chemistry, Proteins genetics
Abstract

Release 4.0 of ProTherm, thermodynamic database for proteins and mutants, contains approximately 14,500 numerical data (approximately 450% of the first version) of several thermodynamic parameters along with experimental methods and conditions, and structural, functional and literature information. The sequence and structural information of proteins is connected with thermodynamic data through links between entries in Protein Data Bank, Protein Information Resource and SWISS-PROT and the data in ProTherm. We have separated the Gibbs free energy change obtained at extrapolated temperature from the data on denaturation temperature measured by the thermal denaturation method. We have added the statistics of amino acid replacements and links to homologous structures to each protein. Further, we have improved the search and display options to enhance search capability through the web interface. ProTherm is freely available at http://gibk26. bse.kyutech.ac.jp/jouhou/Protherm/protherm.html.

Published
2004
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46. Importance of mutant position in Ramachandran plot for predicting protein stability of surface mutations.

Author

Gromiha MM, Oobatake M, Kono H, Uedaira H, and Sarai A

Subjects
Biopolymers chemistry, Drug Stability, Hydrogen Bonding, Protein Conformation, Protein Structure, Secondary, Thermodynamics, Mutation, Proteins chemistry, Proteins genetics
Abstract

Understanding the mechanisms by which mutations affect protein stability is one of the most important problems in molecular biology. In this work, we analyzed the relationship between changes in protein stability caused by surface mutations and changes in 49 physicochemical, energetic, and conformational properties of amino acid residues. We found that the hydration entropy was the major contributor to the stability of surface mutations in helical segments; other properties responsible for size and volume of molecule also correlated significantly with stability. Classification of coil mutations based on their locations in the (phi-psi) map improved the correlation significantly, demonstrating the existence of a relationship between stability and strain energy, which indicates that the role of strain energy is very important for the stability of surface mutations. We observed that the inclusion of sequence and structural information raised the correlation, indicating the influence of surrounding residues on the stability of surface mutations. Further, we examined the previously reported "inverse relationship" between stability and hydrophobicity, and observed that the inverse hydrophobic effect was generally applicable only to coil mutations. The present study leads to a simple method for predicting protein stability changes caused by amino acid substitutions, which will be useful for protein engineering in designing novel proteins with increased stability and altered function., (Copyright 2002 Wiley Periodicals, Inc. Biopolymers 64: 210-220, 2002)

Published
2002
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47. ProTherm, Thermodynamic Database for Proteins and Mutants: developments in version 3.0.

Author

Gromiha MM, Uedaira H, An J, Selvaraj S, Prabakaran P, and Sarai A

Subjects
Animals, Database Management Systems, Information Storage and Retrieval, Internet, Protein Folding, Proteins physiology, Quality Control, Structure-Activity Relationship, Databases, Protein, Mutation, Proteins chemistry, Proteins genetics, Thermodynamics
Abstract

The current release of ProTherm, Thermodynamic Database for Proteins and Mutants, contains more than 10 000 numerical data (300% of the first version) of several thermodynamic parameters, experimental methods and conditions, reversibility of folding, details about the surrounding residues in space for all mutants, structural, functional and literature information. In the current version, we have added information about the source of each protein, identification codes for SWISS-PROT and Protein Information Resource and unique Protein Data Bank (PDB) code for proteins with relevant source. We have also provided additional options to search for data based on PDB code, number of states and reversibility. ProTherm is cross-linked with other sequence, structural, functional and literature databases, and the mutant sites and surrounding residues are automatically mapped on the structure. The ProTherm database is freely available at http://www.rtc.riken.go.jp/jouhou/protherm/protherm.html.

Published
2002
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48. Thermodynamic database for protein-nucleic acid interactions (ProNIT).

Author

Prabakaran P, An J, Gromiha MM, Selvaraj S, Uedaira H, Kono H, and Sarai A

Subjects
Amino Acid Sequence, Bacteriophage lambda genetics, Bacteriophage lambda metabolism, Base Sequence, Computational Biology, Computer Simulation, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Nucleic Acids genetics, Operator Regions, Genetic, Protein Binding, Proteins genetics, Repressor Proteins chemistry, Repressor Proteins genetics, Repressor Proteins metabolism, Software, Thermodynamics, User-Computer Interface, Viral Proteins, Viral Regulatory and Accessory Proteins, DNA-Binding Proteins, Databases, Genetic, Nucleic Acids chemistry, Nucleic Acids metabolism, Proteins chemistry, Proteins metabolism
Abstract

Motivation: Protein-nucleic acid interactions are fundamental to the regulation of gene expression. In order to elucidate the molecular mechanism of protein-nucleic acid recognition and analyze the gene regulation network, not only structural data but also quantitative binding data are necessary. Although there are structural databases for proteins and nucleic acids, there exists no database for their experimental binding data. Thus, we have developed a Thermodynamic Database for Protein-Nucleic Acid Interactions (ProNIT)., Results: We have collected experimentally observed binding data from the literature. ProNIT contains several important thermodynamic data for protein-nucleic acid binding, such as dissociation constant (K(d)), association constant (K(a)), Gibbs free energy change (DeltaG), enthalpy change (DeltaH), heat capacity change (DeltaC(p)), experimental conditions, structural information of proteins, nucleic acids and the complex, and literature information. These data are integrated into a relational database system together with structural and functional information to provide flexible searching facilities by using combinations of various terms and parameters. A www interface allows users to search for data based on various conditions, with different display and sorting options, and to visualize molecular structures and their interactions., Availability: ProNIT is freely accessible at the URL http://www.rtc.riken.go.jp/jouhou/pronit/pronit.html.

Published
2001
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49. Role of hydration of polyhydroxy compounds in biological systems.

Author

Uedaira H and Uedaira H

Subjects
Animals, Asparaginase chemistry, Collagen chemistry, Hemoglobins chemistry, Magnetic Resonance Spectroscopy, Protein Denaturation, Solutions chemistry, Temperature, Alcohols chemistry, Carbohydrates chemistry, Polymers chemistry, Water chemistry
Abstract

The spin-lattice relaxation times, T1, of H2(17)O have been measured for aqueous solutions of 9 polyols as a function of the concentration at 25 degrees C. The dynamic hydration number, nDHN, for polyols were obtained. The values of nDHN increased with an increase in the number of OH groups and depended on the conformation of isomers. The value of nDHN for inositol was the largest. This means that the thermal motion of water molecules around inositol is most inhibited among the polyols studied. The increment of thermal stability of proteins by polyols and sugars, the equilibrium distribution coefficients of polyols and sugars in the denatured hemoglobin solution, and the effect of sugars on the osmotic flow of water were expressed by linear relation of nDHN. On the bases of these relations, a systematic treatment for the effect of hydration of polyols and sugars on these phenomena is discussed.

Published
2001

50. Thermodynamic databases for proteins and protein-nucleic acid interactions.

Author

Sarai A, Gromiha MM, An J, Prabakaran P, Selvaraj S, Kono H, Oobatake M, and Uedaira H

Subjects
Models, Molecular, Models, Theoretical, Mutation, Protein Binding, DNA metabolism, Databases as Topic, Proteins metabolism, RNA metabolism, Thermodynamics
Abstract

Thermodynamic data regarding proteins and their interactions are important for understanding the mechanisms of protein folding, protein stability, and molecular recognition. Although there are several structural databases available for proteins and their complexes with other molecules, databases for experimental thermodynamic data on protein stability and interactions are rather scarce. Thus, we have developed two electronically accessible thermodynamic databases. ProTherm, Thermodynamic Database for Proteins and Mutants, contains numerical data of several thermodynamic parameters of protein stability, experimental methods and conditions, along with structural, functional, and literature information. ProNIT, Thermodynamic Database for Protein-Nucleic Acid Interactions, contains thermodynamic data for protein-nucleic acid binding, experimental conditions, structural information of proteins, nucleic acids and the complex, and literature information. These data have been incorporated into 3DinSight, an integrated database for structure, function, and properties of biomolecules. A WWW interface allows users to search for data based on various conditions, with different display and sorting options, and to visualize molecular structures and their interactions. These thermodynamic databases, together with structural databases, help researchers gain insight into the relationship among structure, function, and thermodynamics of proteins and their interactions, and will become useful resources for studying proteins in the postgenomic era., (Copyright 2002 Wiley Periodicals, Inc.)

Published
2001
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