Effect of Osmolytes on the Exchange Rates of Backbone Amide Protons in Proteins

Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 2969-2978 ◽  
Author(s):  
Rachel L. Foord ◽  
Robin J. Leatherbarrow
Keyword(s):  
Exchange Rates ◽  
Backbone Amide ◽  
Amide Protons

scholarly journals Anion modulation of the1H/2H exchange rates in backbone amide protons monitored by NMR spectroscopy

2007 ◽  
Vol 16 (12) ◽  
pp. 2733-2740 ◽  
Author(s):  
Xavier Tadeo ◽  
David Castaño ◽  
Oscar Millet
Keyword(s):  
Nmr Spectroscopy ◽  
Exchange Rates ◽  
Backbone Amide ◽  
Amide Protons

ChemInform Abstract: Exchange Rates of the Amide Protons of d-Biotin Sulfoxide Stereoisomers

ChemInform ◽  
1987 ◽  
Vol 18 (32) ◽  
Author(s):  
T. L. FOX ◽  
P. A. TIPTON ◽  
W. W. CLELAND ◽  
A. S. MILDVAN
Keyword(s):  
Exchange Rates ◽  
Abstract Exchange ◽  
Amide Protons

scholarly journals Direct and Indirect Models for Protein Chemical Denaturation are Characteristic of Opposite Dynamic Properties

2016 ◽  
Author(s):  
Liangzhong Lim ◽  
Linlin Miao ◽  
Jianxing Song
Keyword(s):  
Quantitative Analysis ◽  
Exchange Rates ◽  
Dynamic Properties ◽  
Conformational State ◽  
Backbone Dynamics ◽  
Dependent Manner ◽  
Chemical Denaturation ◽  
Concentration Dependent Manner ◽  
Denaturant Concentration ◽  
Amide Protons

AbstractTwo major models, namely direct and indirect models, have been proposed for the protein chemical denaturation but it remains challenging to experimentally demonstrate and distinguish between them. Here, by use of CD and NMR spectroscopy, we succeeded in differentiating the effects on a small but well-folded protein WW4, of GdmCl and NaSCN at diluted concentrations (≥200 mM). Both denaturants up to 200 mM have no alternation of its average structure but do reduce its thermodynamic stability to different degrees. Despite acting as the stronger denaturant, GdmCl only weakly interacts with amide protons, while NaSCN shows extensive interactions with both hydrophobic side chains and amide protons. Although both denaturants show no significant perturbation on overall ps-ns backbone dynamics of WW4, GdmCl suppresses while NaSCN enhances its μs-ms backbone dynamics in a denaturant concentration dependent manner. Quantitative analysis reveals that although they dramatically raise exchange rates, GdmCl slightly increases while NaSCN reduces the population of the major conformational state. Our study represents the first report deciphering that GdmCl and NaSCN appear to destabilize a protein following two models respectively, which are characteristic of opposite μs-ms dynamics.

Measurement of intrinsic exchange rates of amide protons in a 15N-labeled peptide

1995 ◽  
Vol 6 (3) ◽  
Author(s):  
Shohei Koide ◽  
Wolfgang Jahnke ◽  
PeterE. Wright
Keyword(s):  
Exchange Rates ◽  
Amide Protons

pKaShift Effects on Backbone Amide Base-Catalyzed Hydrogen Exchange Rates in Peptides

1998 ◽  
Vol 120 (15) ◽  
pp. 3735-3738 ◽  
Author(s):  
Federico Fogolari ◽  
Gennaro Esposito ◽  
Paolo Viglino ◽  
James M. Briggs ◽  
J. Andrew McCammon
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Backbone Amide
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