Search

Your search keyword '"Goc, Gunce"' showing total 9 results
Start Over Author "Goc, Gunce"
9 results on '"Goc, Gunce"'

4. Cryogenic X-ray crystallographic studies of biomacromolecules at Turkish Light Source “Turkish DeLight”

Author

Atalay, Necati; Akcan, Enver Kamil; Gül, Mehmet; Ayan, Esra; Destan, Ebru; Ertem, Fatma Betül; Tokay, Nurettin; Çakılkaya, Barış; Nergiz, Zeliş; Karakadıoğlu, Gözde; Kepçeoğlu, Abdullah; Yapıcı, İlkin; Tosun, Bilge; Baldır, Nilüfer; Yıldırım, Günseli; Johnson, Jerome Austin; Güven, Ömür; Shafiei, Alaleh; Arslan, Nazlı Eylül; Yılmaz, Merve; Kulakman, Cahine; Paydos, Seyide Seda; Çinal, Zeynep Sena; Şabanoğlu, Kardelen; Pazarçeviren, Ayşegül; Yılmaz, Ayşenur; Canbay, Başak; Aşcı, Bengisu; Kartal, Esra; Tavlı, Serra; Çiftçi, Halil İbrahim; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Caliseki, Mehmet; Goc, Gunce; Mermer, Arif; Yesilay, Gamze; Altuntas, Sevde; Tateishi, Hiroshi; Otsuka, Masami; Fujita, Mikako; Tekin, Saban; Durdagi, Serdar; Doganay, Gizem Dinler; Karaca, Ezgi; Turkoz, Burcu Kaplan; Kabasakal, Burak Veli; Kati, Ahmet, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering, Atalay, Necati; Akcan, Enver Kamil; Gül, Mehmet; Ayan, Esra; Destan, Ebru; Ertem, Fatma Betül; Tokay, Nurettin; Çakılkaya, Barış; Nergiz, Zeliş; Karakadıoğlu, Gözde; Kepçeoğlu, Abdullah; Yapıcı, İlkin; Tosun, Bilge; Baldır, Nilüfer; Yıldırım, Günseli; Johnson, Jerome Austin; Güven, Ömür; Shafiei, Alaleh; Arslan, Nazlı Eylül; Yılmaz, Merve; Kulakman, Cahine; Paydos, Seyide Seda; Çinal, Zeynep Sena; Şabanoğlu, Kardelen; Pazarçeviren, Ayşegül; Yılmaz, Ayşenur; Canbay, Başak; Aşcı, Bengisu; Kartal, Esra; Tavlı, Serra; Çiftçi, Halil İbrahim; Demirci, Hasan (ORCID 0000-0002-9135-5397 & YÖK ID 307350), Caliseki, Mehmet; Goc, Gunce; Mermer, Arif; Yesilay, Gamze; Altuntas, Sevde; Tateishi, Hiroshi; Otsuka, Masami; Fujita, Mikako; Tekin, Saban; Durdagi, Serdar; Doganay, Gizem Dinler; Karaca, Ezgi; Turkoz, Burcu Kaplan; Kabasakal, Burak Veli; Kati, Ahmet, Koç Üniversitesi İş Bankası Enfeksiyon Hastalıkları Uygulama ve Araştırma Merkezi (EHAM) / Koç University İşbank Center for Infectious Diseases (KU-IS CID), Graduate School of Sciences and Engineering; College of Sciences, and Department of Molecular Biology and Genetics; Department of Chemical and Biological Engineering

Abstract

X-ray crystallography is a robust and powerful structural biology technique that provides high-resolution atomic structures of biomacromolecules. Scientists use this technique to unravel mechanistic and structural details of biological macromolecules (e.g., proteins, nucleic acids, protein complexes, protein-nucleic acid complexes, or large biological compartments). Since its inception, single-crystal cryocrystallography has never been performed in Türkiye due to the lack of a single-crystal X-ray diffractometer. The X-ray diffraction facility recently established at the University of Health Sciences, İstanbul, Türkiye will enable Turkish and international researchers to easily perform high-resolution structural analysis of biomacromolecules from single crystals. Here, we describe the technical and practical outlook of a state-of-the-art home-source X-ray, using lysozyme as a model protein. The methods and practice described in this article can be applied to any biological sample for structural studies. Therefore, this article will be a valuable practical guide from sample preparation to data analysis., NSF Science and Technology Center Grant; Biology with X-ray Lasers, BioXFEL; Scientific and Technological Research Council of Turkey (TÜBİTAK); TÜBİTAK 2218 - National Postdoctoral Research Fellowship Program; TÜBİTAK 2232 International Outstanding Researchers Program; 2232 International Fellowship for Outstanding Researchers Program; European Union (EU); Horizon 2020; 2236 CoCirculation2 Program; TÜBİTAK 1001 Scientific and Technological Research Projects Funding Program

Published
2023

8. Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.

Author

Yuzugullu Karakus, Yonca, Goc, Gunce, Balci, Sinem, Yorke, Briony A., Trinh, Chi H., McPherson, Michael J., and Pearson, Arwen R.

Subjects
*SCYTALIDIUM, *CRYSTAL structure, *BINDING sites
Abstract

The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3‐amino‐1,2,4‐triazole (3TR) was determined at 1.95 Å resolution. Surprisingly, no binding to the heme site was observed; instead, 3TR occupies a binding site corresponding to the NADPH‐binding pocket in mammalian catalases at the entrance to a lateral channel leading to the heme. Kinetic analysis of site‐directed mutants supports the assignment of this pocket as the binding site for oxidase substrates. [ABSTRACT FROM AUTHOR]

Published
2018
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results