Backbone dynamics of a model membrane protein: measurement of individual amide hydrogen-exchange rates in detergent-solubilized M13 coat protein using carbon-13 NMR hydrogen/deuterium isotope shifts

Biochemistry ◽  
1987 ◽  
Vol 26 (12) ◽  
pp. 3626-3634 ◽  
Author(s):  
Gillian D. Henry ◽  
Joel H. Weiner ◽  
Brian D. Sykes
Keyword(s):  
Coat Protein ◽  
Membrane Protein ◽  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Model Membrane ◽  
Backbone Dynamics ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange ◽  
Hydrogen Deuterium ◽  
Protein Measurement

Determination of amide hydrogen exchange rates in peptides by mass spectrometry

1992 ◽  
Vol 64 (20) ◽  
pp. 2456-2458 ◽  
Author(s):  
Geraldine. Thevenon-Emeric ◽  
John. Kozlowski ◽  
Zhongqi. Zhang ◽  
David L. Smith
Keyword(s):  
Mass Spectrometry ◽  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange

15N Isotopic Labeling and Amide Hydrogen Exchange Rates of Oxidized Iso-1-cytochromec

1997 ◽  
Vol 119 (41) ◽  
pp. 9899-9900 ◽  
Author(s):  
Susan M. Baxter ◽  
Terry L. Boose ◽  
Jacquelyn S. Fetrow
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Isotopic Labeling ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange

Solution Conformation of Peptides through 1H Nuclear Magnetic Double Resonance Measurement of Amide Hydrogen Exchange Rates: Study of the Active Pentapeptide Fragment of Thymopoietin

1980 ◽  
Vol 34 (4) ◽  
pp. 460-464 ◽  
Author(s):  
N. Rama Krishna ◽  
D. H. Huang ◽  
Gideon Goldstein
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Dynamic Equilibrium ◽  
Double Resonance ◽  
Saturation Recovery ◽  
Labile Hydrogen ◽  
Amide Hydrogen ◽  
Thymic Hormone ◽  
Amide Hydrogen Exchange ◽  
Selective Saturation

The amide hydrogen exchange rates of peptides (and other biomolecules) can be related to their secondary and tertiary structures. The exchange rates in the range ∼0.1 to ∼100 s−1 can be conveniently measured in H2O by a double resonance technique involving a combination of two separate 1H NMR experiments: (1) the transfer of solvent saturation and (2) the selective saturation recovery of the labile hydrogen. When a peptide exists in a dynamic equilibrium among several conformations, the interpretation of the above two experiments in terms of intrinsic exchange rates is not straightforward in general. The effect of a multistate conformational averaging is considered in the interpretation of the above two experiments, and analytical expressions have been presented for a few limiting cases of conformational and chemical equilibria. The amide hydrogen exchange rates of the pentapeptide Arg-Lys-Asp-Val-Tyr, the active fragment of the thymic hormone thymopoietin, have been measured in H2O through the transfer of solvent saturation and saturation recovery experiments. The results suggest that this fragment exists in a highly motile dynamic equilibrium among several conformations. In some of these, the Val4 NH hydrogen is shielded significantly from the solvent.

Measurement of amide hydrogen exchange rates with the use of radiation damping

2011 ◽  
Vol 51 (1-2) ◽  
pp. 151-162 ◽  
Author(s):  
Jing-Song Fan ◽  
Jackwee Lim ◽  
Binhan Yu ◽  
Daiwen Yang
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Radiation Damping ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange

Amide hydrogen exchange rates of model peptides in dimethyl sulphoxide solutions

Tetrahedron ◽  
1986 ◽  
Vol 42 (17) ◽  
pp. 4743-4756 ◽  
Author(s):  
J. Chrisment ◽  
J.J. Delpuech ◽  
W. Rajerison ◽  
C. Selve
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Dimethyl Sulphoxide ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange ◽  
Model Peptides

Global Changes in Amide Hydrogen Exchange Rates for a Protein Antigen in Complex with Three Different Antibodies

1996 ◽  
Vol 257 (4) ◽  
pp. 866-876 ◽  
Author(s):  
David C. Williams Jr ◽  
David C. Benjamin ◽  
Roberto J. Poljak ◽  
Gordon S. Rule
Keyword(s):  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Protein Antigen ◽  
Global Changes ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange
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