Proline isomerization is widely recognized as a kinetic bottleneck in protein folding, amplified for proteins rich in Pro residues. We introduced repeated hydrostatic pressure jumps between native and pressure-denaturing conditions inside an NMR sample cell to study proline isomerization in the pressure-sensitized L50A ubiquitin mutant. Whereas in two unfolded heptapeptides, X-Pro peptide bonds isomerized ca 1.6-fold faster at 1 bar than at 2.5 kbar, for ubiquitin ca eight-fold faster...
[ASAP] Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR
Cyril Charlier, Joseph M. Courtney, T. Reid Alderson, Philip Anfinrud, Ad Bax
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b04833/20180625/images/medium/ja-2018-04833s_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b04833
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http://feeds.feedburner.com/~r/acs/jacsat/~4/Wf5C6etrn-c
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06-25-2018 11:22 PM
[NMR paper] Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR.
J Am Chem Soc. 2018 Jun 20;:
Authors: Charlier C, Courtney JM, Alderson TR, Anfinrud P, Bax A
Abstract
Novel pressure-jump NMR hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. While protein...
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06-21-2018 10:11 PM
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the...
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05-01-2018 10:57 PM
[NMR paper] Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Related Articles Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Proc Natl Acad Sci U S A. 2018 Apr 16;:
Authors: Charlier C, Alderson TR, Courtney JM, Ying J, Anfinrud P, Bax A
Abstract
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded...
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04-19-2018 01:52 PM
[NMR paper] Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
Related Articles Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.
J Am Chem Soc. 2017 Aug 02;:
Authors: Alderson TR, Charlier C, Torchia DA, Anfinrud P, Bax A
Abstract
A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly dropping the hydrostatic pressure inside the NMR sample cell from denaturing...
Effect of Internal Cavities on Folding Rates and RoutesRevealed by Real-Time Pressure-Jump NMR Spectroscopy
Effect of Internal Cavities on Folding Rates and RoutesRevealed by Real-Time Pressure-Jump NMR Spectroscopy
Julien Roche, Mariano Dellarole, Jose? A. Caro, Douglas R. Norberto, Angel E. Garcia, Bertrand Garcia-Moreno, Christian Roumestand and Catherine A. Royer
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja406682e/aop/images/medium/ja-2013-06682e_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja406682e
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09-19-2013 02:19 PM
[NMR paper] Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
J Am Chem Soc. 2013 Aug 30;
Authors: Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno E B, Roumestand C, Royer CA
Abstract
The time required to fold proteins usually increases significantly under conditions of high pressure. Taking advantage of this general property of proteins, we combined P-jump...