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Your search keyword '"Broxterman, Q. A."' showing total 175 results
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175 results on '"Broxterman, Q. A."'

2. New developments in the chemo-enzymatic production of amino acids

Author

Kamphuis, J., Boesten, W. H. J., Broxterman, Q. B., Hermes, H. F. M., van Balken, J. A. M., Meijer, E. M., Schoemaker, H. E., Fiechter, A., editor, Aiba, S., editor, Bungay, H. R., editor, Cooney, Ch L., editor, Demain, A. L., editor, Fukui, S., editor, Kieslich, K., editor, Klibanov, A. M., editor, Lafferty, R. M., editor, Primrose, S. B., editor, Rehm, H. J., editor, Rogers, P. L., editor, Sahm, H., editor, Schügerl, K., editor, Suzuki, S., editor, Tsao, G. T., editor, Venkat, K., editor, and Winnacker, E. -L., editor

Published
1990
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16. Ca-methyl, Ca-n-propylglycine homo-oligomers

Author

FORMAGGIO F., CRISMA M., TONIOLO C., BROXTERMAN Q. B., KAPTEIN B., CORBIER C., SAVIANO M., PALLADINO P., BENEDETTI, ETTORE, Formaggio, F, Crisma, M, Toniolo, C, Broxterman, Q. B., Kaptein, B, Corbier, C, Saviano, Michele, Palladino, P, Benedetti, E., Formaggio, F., Crisma, M., Toniolo, C., Kaptein, B., Corbier, C., Saviano, M., Palladino, P., and Benedetti, Ettore

Abstract

A series of Na-protected, monodispersed homo-oligopeptide esters to the octamer level from L-Ca-Me, Ca-propylglycine [or Ca-methylnorvaline, (aMe)Nva] has been synthesized by soln. methods and fully characterized. The preferred conformation of these homo-oligomers in soln. has been assessed by FT-IR absorption and 1H NMR techniques. Moreover, the mol. structures of the homotrimer and homotetramer have been detd. in the crystal state by X-ray diffraction. The obtained results strongly support the view that right-handed, single or multiple, and consecutive b bends are preferentially adopted by the conformationally restricted L-(aMe)Nva homo-oligomers. In particular, 310 helixes are formed by the longest homo-oligomers. It is our contention that the [(aMe)Nva]n peptides represent the best available choice among Ca-tetrasubstituted a-amino acid-based homo-oligomers for the construction of relatively easy to make, rigid foldamers with a well-defined screw-sense bias.

Published
2003

17. Ca,a-Methyl,Ca,a-allylglycine (Mag) Homooligomers

Author

PEGGION C, FORMAGGIO F, CRISMA M, TONIOLO C, KAMPHUIS J, KAPTEIN B, BROXTERMAN Q. N, VITALE R. M, IACOVINO R, BENEDETTI E., SAVIANO, MICHELE, Peggion, C, Formaggio, F, Crisma, M, Toniolo, C, Kamphuis, J, Kaptein, B, Broxterman, Q. N., Vitale, R. M., Iacovino, R, Saviano, Michele, and Benedetti, E.

Published
2001

22. Linear oligopeptide. Part 406. Helical screw sense of peptide molecules: the penatpeptide system (AiB)4/LVal[L-(alphaMe)Val] in solution

Author

Pengo B., Formaggio F., Crisma M., Toniolo C., Bonora G. M., Broxterman Q. B., Kamphiuis J., Saviano M., Iacovino R., ROSSI, FILOMENA, BENEDETTI, ETTORE, Pengo, B., Formaggio, F., Crisma, M., Toniolo, C., Bonora, G. M., Broxterman, Q. B., Kamphiuis, J., Saviano, M., Iacovino, R., Rossi, Filomena, and Benedetti, Ettore

Subjects
Chiral valine, 10 helical helical structure, FTIR, NMR, CD
Abstract

We reported the conformational analisis carried out by CD, FTIR and NMR for N-blocked pentapetide esters containing four helicogenic alpha aminoisobutyric acid residue and one chiral valine. The results showed that all pentapetides examined fold into a 3,10 helical structure.

Published
1998

36. C-alpha-Methyl Norvaline Foldamers

Author

Formaggio, F., Crisma, M., Toniolo, C., Broxterman, Q. B., Kaptein, B., Corbier, C., Saviano, M., Pasquale Palladino, and Benedetti, E.

Published
2004

37. Cα-Methyl Norvaline Foldamers

Author

Formaggio, Fernando, Crisma, M., Toniolo, Claudio, Broxterman, Q. B., Kaptein, B., Corbier, C., Saviano, M., Palladino, P., and Benedetti, E.

Published
2004

39. Cβ-Methyl, Cβ-phenylglycine peptides

Author

Doi, M., primary, Ishida, T., additional, Mossel, E., additional, Formaggio, F., additional, Crisma, M., additional, Toniolo, C., additional, Broxterman, Q. B., additional, and Kamphuis, J., additional

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40. Quantitative Correlation of Solvent Polarity with the ?Ñ-/310-Helix Equilibrium: A Heptapeptide Behaves as a Solvent-Driven Molecular Spring

Author

Pengo P., Pasquato L., Moro S., Brigo A., Fogolari F., Broxterman Q. B., Kaptein B., and Scrimin P.

Abstract

The paper describes compelling experimental evidence of the reversible interconversion of an heptapeptide between two helical conformations and provides a rationale for the phenomenon, i.e. the polarity of the solvent. It also demonstrates that the dependence from this latter parameter is not just qualitative but quantitative. The reversibility of the process indicates that the heptapeptide behaves like a molecular spring when it is dissolved in solvents of different polarity: in fact its lengths varies from 15 to 17 Å as it switches from the alpha- to the 310-helix conformation. Several molecular calculations had suggested that the experiments that we illustrate for the first time here should indeed happen. However, the difficulty in finding a short peptide highly folded with an helical conformation had hampered the possibility to verify those computational indications. These results have relevant consequences for the interpretation of structural phenomena occurring in the active/recognition sites of enzymes

Published
2003

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