[NMR paper] The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
Related Articles The Energetics of a Three-State Protein Folding System Probed by High-Pressure Relaxation Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Sep 14;54(38):11157-11161
Authors: Tugarinov V, Libich DS, Meyer V, Roche J, Clore GM
Abstract
The energetic and volumetric properties of a three-state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been...
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[NMR paper] Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Related Articles Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.
Subcell Biochem. 2015;72:261-278
Authors: Roche J, Dellarole M, Royer CA, Roumestand C
Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of...
[NMR images] in vitro protein folding
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in vitro protein folding
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03-20-2014 12:44 PM
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
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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[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...
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08-31-2013 06:56 PM
[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Methods. 2004 Sep;34(1):133-43
Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K
Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...
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[NMR paper] Cooperativity of a protein folding reaction probed at multiple chain positions by rea
Cooperativity of a protein folding reaction probed at multiple chain positions by real-time 2D NMR spectroscopy.
Related Articles Cooperativity of a protein folding reaction probed at multiple chain positions by real-time 2D NMR spectroscopy.
Biochemistry. 2000 Jul 11;39(27):7910-9
Authors: Steegborn C, Schneider-Hassloff H, Zeeb M, Balbach J
The refolding reaction of S54G/P55N ribonuclease T1 is a two-step process, where fast formation of a partly folded intermediate is followed by the slow reaction to the native state, limited by a trans -->...