The earliest events in the folding of a protein are in general poorly understood. We used NMR R(2) relaxation dispersion experiments to study transient local collapse events in the unfolded-state (U) conformational ensemble of apomyoglobin (apoMb). Local residual secondary structure (seen in regions corresponding to the A, D, E, and H helices of the folded protein) is largely unchanged over the pH range of 2.3-2.75, yet a significant pH-dependent increase in the conformational exchange...
[NMR paper] Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
J Am Chem Soc. 2017 Jan 11;:
Authors: Franco R, Gil-Caballero S, Ayala I, Favier A, Brutscher B
Abstract
NMR spectroscopy is a powerful tool for studying...
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[NMR paper] Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.
Angew Chem Int Ed Engl. 2014 Apr 22;53(17)
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J,...
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[NMR paper] Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Related Articles Probing Transient Conformational States of Proteins by Solid-State R1? Relaxation-Dispersion NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Mar 18;
Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P
Abstract
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally...
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Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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[NMR paper] Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Related Articles Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Nature. 2004 Jul 29;430(6999):586-90
Authors: Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE
Many biochemical processes proceed through the formation of functionally significant intermediates. Although the identification and characterization of such species can provide vital clues about the mechanisms of the...
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11-24-2010 09:51 PM
[NMR paper] A protein folding intermediate of ribonuclease T1 characterized at high resolution by
A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy.
Related Articles A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy.
J Mol Biol. 1999 Jan 15;285(2):829-42
Authors: Balbach J, Steegborn C, Schindler T, Schmid FX
The rate-limiting step during the refolding of S54G/P55N ribonuclease T1 is determined by the slow trans-->cis prolyl isomerisation of Pro39. We investigated the refolding of this variant by...
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A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Sec
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Securities Industry News (blog) (subscription)
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A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Securities Industry News (blog) (subscription)
In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, ...
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Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion
Linear Mode
