Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation

Biochemistry ◽  
1992 ◽  
Vol 31 (5) ◽  
pp. 1263-1269 ◽  
Author(s):  
Carol A. Rohl ◽  
J. Martin Scholtz ◽  
Eunice J. York ◽  
John M. Stewart ◽  
Robert L. Baldwin
Keyword(s):  
Proton Exchange ◽  
Amide Proton ◽  
Helical Peptides ◽  
Amide Proton Exchange ◽  
Chain Lengths ◽  
Kinetics Of

Kinetics of Rapid Reactions in Liquid Ammonia. The Ammonia—Amide Proton Exchange

1966 ◽  
Vol 44 (7) ◽  
pp. 2797-2801 ◽  
Author(s):  
T. J. Swift ◽  
S. B. Marks ◽  
W. G. Sayre
Keyword(s):  
Liquid Ammonia ◽  
Proton Exchange ◽  
Amide Proton ◽  
Amide Proton Exchange ◽  
Kinetics Of

scholarly journals Amide proton exchange of a dynamic loop in cell extracts

2013 ◽  
Vol 22 (10) ◽  
pp. 1313-1319 ◽  
Author(s):  
Austin E. Smith ◽  
Mohona Sarkar ◽  
Gregory B. Young ◽  
Gary J. Pielak
Keyword(s):  
Proton Exchange ◽  
Amide Proton ◽  
Amide Proton Exchange ◽  
Cell Extracts

scholarly journals In-Situ Flexibility of Both Redox-States of the Chloroplast Regulatory Protein CP12

2021 ◽  
Author(s):  
Helene Launay ◽  
Hui Shao ◽  
Olivier Bornet ◽  
Francois-Xavier Cantrelle ◽  
Regine Lebrun ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Cell Extract ◽  
Proton Exchange ◽  
Conformational Exchange ◽  
Amide Proton ◽  
Cysteine Residues ◽  
Intrinsically Disordered ◽  
Amide Proton Exchange ◽  
C Terminus ◽  
Helical Turn

In the chloroplast, Calvin-Benson-Bassham enzymes are active in the reducing environment imposed in the light via the electrons from the photosystems. In the dark these enzymes are inhibited, and this regulation is mainly mediated via oxidation of key regulatory cysteine residues. CP12 is a small protein that plays a role in this regulation with four cysteine residues that undergo a redox transition. Using amide-proton exchange with solvent measured by nuclear magnetic resonance (NMR) and mass-spectrometry, we confirmed that reduced CP12 is intrinsically disordered. Using real-time NMR, we showed that the oxidation of the two disulfide bridges are simultaneous. In oxidized CP12, the C23-C31 pair is in a region that undergoes a conformational exchange in the NMR-intermediate timescale. The C66-C75 pair is in the C-terminus that folds into a stable helical turn. We confirmed that these structural states exist in a physiologically relevant environment that is, in cell extract from Chlamydomonas reinhardtii. Consistent with these structural equilibria, the reduction is slower for the C66-C75 pair compared to the C23-C31 pair. Finally, the redox mid-potentials for the two cysteine pairs differ and are similar to those found for phosphoribulokinase and glyceraldehyde 3-phosphate dehydrogenase, that we relate to the regulatory role of CP12.

Investigation of Protein Amide-Proton Exchange by 1H Longitudinal Spin Relaxation

1995 ◽  
Vol 108 (3) ◽  
pp. 220-234 ◽  
Author(s):  
Z.W. Zheng ◽  
M.R. Gryk ◽  
M.D. Finucane ◽  
O. Jardetzky
Keyword(s):  
Spin Relaxation ◽  
Proton Exchange ◽  
Amide Proton ◽  
Amide Proton Exchange ◽  
Longitudinal Spin
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