[NMR paper] Proline Peptide Bond Isomerization in Ubiquitin under Folding and Denaturing Conditions by Pressure-Jump NMR
Proline Peptide Bond Isomerization in Ubiquitin under Folding and Denaturing Conditions by Pressure-Jump NMR
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...
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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[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...
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Chembiochem. 2013 Jun 28;
Authors: Roche J, Ying J, Maltsev AS, Bax A
Abstract
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell - pnas.org
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