Regional stability changes in oxidized and reduced cytochrome c located by hydrogen exchange and mass spectrometry
- 1 October 1997
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Society for Mass Spectrometry
- Vol. 8 (10) , 1039-1045
- https://doi.org/10.1016/s1044-0305(97)00150-5
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- A statistical mechanical model for hydrogen exchange in globular proteinsProtein Science, 1995
- Protein stability parameters measured by hydrogen exchangeProteins-Structure Function and Bioinformatics, 1994
- Hydrogen exchange identifies native-state motional domains important in protein foldingBiochemistry, 1993
- An Antibody Binding Site on Cytochrome C Defined by Hydrogen Exchange and Two-Dimensional NMRScience, 1990
- NMR evidence for an early framework intermediate on the folding pathway of ribonuclease ANature, 1988
- Two-dimensional proton NMR studies of cytochrome c: hydrogen exchange in the N-terminal helixBiochemistry, 1986
- Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protonsProteins-Structure Function and Bioinformatics, 1986
- Hydrogen exchange and structural dynamics of proteins and nucleic acidsQuarterly Reviews of Biophysics, 1983
- Hydrogen exchange and the dynamic structure of proteinsMolecular and Cellular Biochemistry, 1982
- Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitorBiophysical Journal, 1980