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

Shohei Koide; Wolfgang Jahnke; PeterE. Wright

doi:10.1007/bf00197811

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

ChemInform ◽

10.1002/chin.198732069 ◽

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

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

10.1101/073346 ◽

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.

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

Biochemistry ◽

10.1021/bi9712798 ◽

1998 ◽

Vol 37 (9) ◽

pp. 2969-2978 ◽

Cited By ~ 42

Author(s):

Rachel L. Foord ◽

Robin J. Leatherbarrow

Keyword(s):

Exchange Rates ◽

Backbone Amide ◽

Amide Protons

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Measurement of Very Fast Exchange Rates of Individual Amide Protons in Proteins by NMR Spectroscopy

ChemPhysChem ◽

10.1002/cphc.201801044 ◽

2018 ◽

Vol 20 (2) ◽

pp. 231-235 ◽

Cited By ~ 6

Author(s):

Rupashree Dass ◽

Enrico Corlianò ◽

Frans A. A. Mulder

Keyword(s):

Nmr Spectroscopy ◽

Exchange Rates ◽

Fast Exchange ◽

Amide Protons

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Exchange rates of the amide protons of d-biotin sulfoxide stereoisomers

Journal of the American Chemical Society ◽

10.1021/ja00241a033 ◽

1987 ◽

Vol 109 (7) ◽

pp. 2127-2129 ◽

Cited By ~ 3

Author(s):

Terry L. Fox ◽

Peter A. Tipton ◽

W. W. Cleland ◽

Albert S. Mildvan

Keyword(s):

Exchange Rates ◽

Amide Protons

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NMR measurements of proton exchange between solvent and peptides and proteins.

Acta Biochimica Polonica ◽

10.18388/abp.1999_4137 ◽

1999 ◽

Vol 46 (3) ◽

pp. 651-663 ◽

Cited By ~ 4

Author(s):

J Wójcik ◽

K Ruszczyńska ◽

I Zhukov ◽

A Ejchart

Keyword(s):

Exchange Rates ◽

Magnetization Transfer ◽

Deuterium Exchange ◽

Proton Exchange ◽

Hydrogen Deuterium Exchange ◽

Hydrogen Deuterium ◽

Transfer Method ◽

Amide Protons

Scope and limitations of the NMR based methods, equilibration and magnetization transfer, for measuring proton exchange rates of amide protons in peptides and proteins with water protons are discussed. Equilibration is applied to very slow processes detected by hydrogen-deuterium exchange after a solute is dissolved in D2O. Magnetization transfer allows to study moderately rapid processes in H2O. A number of precautions should be undertaken in order to avoid systemic errors inherent in the magnetization transfer method.

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