scholarly journals Amide proton exchange measurements as a probe of the stability and dynamics of the n-terminal domain of the ribosomal protein L9: Comparison with the intact protein

1998 ◽  
Vol 7 (9) ◽  
pp. 1994-1997 ◽  
Author(s):  
Liliya Vugmeyster ◽  
Brian Kuhlman ◽  
Daniel P. Raleigh
Keyword(s):  
Ribosomal Protein ◽  
Proton Exchange ◽  
Amide Proton ◽  
Intact Protein ◽  
Terminal Domain ◽  
Amide Proton Exchange ◽  
Ribosomal Protein L9 ◽  
The Stability

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

Corrections - Influence of Charge on the Rate of Amide Proton Exchange

Biochemistry ◽  
1982 ◽  
Vol 21 (12) ◽  
pp. 3036-3036 ◽  
Author(s):  
Peter Kim ◽  
Robert Baldwin
Keyword(s):  
Proton Exchange ◽  
Amide Proton ◽  
Amide Proton Exchange
Sign in / Sign up

Export Citation Format

Share Document