Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys-14 and Cys-38. Influence of Charged Protecting Groups on the Stability of the Protein-Reference-Cited by-同舟云学术

Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys-14 and Cys-38. Influence of Charged Protecting Groups on the Stability of the Protein

Published:1979-04 Issue:2 Volume:95 Page:249-253
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

WAGNER Gerhard,KALB (GILBOA) A. Joseph,WUTHRICH Kurt

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1979.tb12960.x/fullpdf

Reference15 articles.

1. The X-Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides

2. Nmr studies of the molecular conformations in the linear oligopeptides H-(L-Ala)n-L-Pro-OH

3. 3. R. Hetzel (1978 ) Ph.D. Thesis , no. 6125, ETH Zurich.

4. A 1H Nuclear-Magnetic-Resonance Study of the Conformation and the Molecular Dynamics of the Glycoprotein Cow-Colostrum Trypsin Inhibitor

5. The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor

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