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

scholarly journals Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

2008 ◽  
Vol 6 (10) ◽  
pp. 2203-2217 ◽  
Author(s):  
Zhongqi Zhang ◽  
Weiqun Li ◽  
Timothy M. Logan ◽  
Ming Li ◽  
Alan G. Marshall
Keyword(s):  
Mass Spectrometry ◽  
Exchange Rates ◽  
Hydrogen Exchange ◽  
Binding Protein ◽  
Amide Hydrogen ◽  
Amide Hydrogen Exchange ◽  
Fk506 Binding Protein

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.

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