Related ArticlesAn 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
J Am Chem Soc. 2005 Apr 13;127(14):5066-72
Authors: Choy WY, Zhou Z, Bai Y, Kay LE
15N relaxation dispersion NMR spectroscopy has been used to study exchange dynamics in a pair of mutants of Rd-apocyt b562, a redesigned four-helix-bundle protein. An analysis of the relaxation data over a range of temperatures establishes that exchange in both proteins is best modeled as two-state and that it derives from the folding/unfolding transition. These results are in accord with predictions based on the reaction coordinate for the folding of the protein determined from native-state hydrogen exchange data [Chu, R.; Pei, W.; Takei, J.; Bai, Y. Biochemistry 2002, 41, 7998-8003]. The kinetics and thermodynamics of the folding transition have been characterized in detail. Although only a narrow range of temperatures could be examined, it is clear that the folding rate temperature profile is distinctly non-Arrhenius for both mutants, with the folding barrier for at least one of them entropic.
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
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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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06-07-2011 11:05 AM
[NMR paper] NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
Related Articles NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
J Am Chem Soc. 2005 Sep 28;127(38):13207-12
Authors: Zeeb M, Balbach J
The cold shock protein CspB adopts its native and functional tertiary structure on the millisecond time scale. We employed transverse relaxation NMR methods, which allow a quantitative measurement of the cooperativity of this...
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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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[NMR paper] NMR spin relaxation methods for characterization of disorder and folding in proteins.
NMR spin relaxation methods for characterization of disorder and folding in proteins.
Related Articles NMR spin relaxation methods for characterization of disorder and folding in proteins.
J Mol Graph Model. 2001;19(1):3-12
Authors: Bracken C
The flexibility and dynamics of proteins directly influence the processes of protein folding, recognition, and function. NMR spin relaxation methods are used to assess the dynamics and mobility of proteins, for fast ps and ns motions as well as slower microsecond and ms events. The degree of protein...
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Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Water-Proton-Spin-Lattice-Relaxation Dispersion of Paramagnetic Protein Solutions
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 November 2010</br>
Galina, Diakova , Yanina, Goddard , Jean-Pierre, Korb , Robert G., Bryant</br>
The paramagnetic contributions to water proton spin-lattice relaxation rate constants in protein systems spin-labeled with nitroxide radicals were re-examined. As noted by others, the strength of the dipolar coupling between water protons and the protein-bound nitroxide radical often appears to...
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[NMR paper] A 31P-NMR spin-lattice relaxation and 31P[1H] nuclear Overhauser effect study of soni
A 31P-NMR spin-lattice relaxation and 31P nuclear Overhauser effect study of sonicated small unilamellar phosphatidylcholine vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 31P-NMR spin-lattice relaxation and 31P nuclear Overhauser effect study of sonicated small unilamellar phosphatidylcholine vesicles.
Biochim Biophys Acta. 1992 Feb 17;1104(1):137-46
Authors: Tauskela JS, Thompson M
The motional properties of the inner and outer monolayer headgroups of...
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Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
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Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....
An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mu
Linear Mode
