Related ArticlesNMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
Proc Natl Acad Sci U S A. 2013 Jul 18;
Authors: Sekhar A, Kay LE
Abstract
The importance of dynamics to biomolecular function is becoming increasingly clear. A description of the structure-function relationship must, therefore, include the role of motion, requiring a shift in paradigm from focus on a single static 3D picture to one where a given biomolecule is considered in terms of an ensemble of interconverting conformers, each with potentially diverse activities. In this Perspective, we describe how recent developments in solution NMR spectroscopy facilitate atomic resolution studies of sparsely populated, transiently formed biomolecular conformations that exchange with the native state. Examples of how this methodology is applied to protein folding and misfolding, ligand binding, and molecular recognition are provided as a means of illustrating both the power of the new techniques and the significant roles that conformationally excited protein states play in biology.
PMID: 23868852 [PubMed - as supplied by publisher]
Real-Time NMR Characterizationof Structure and Dynamicsin a Transiently Populated Protein Folding Intermediate
Real-Time NMR Characterizationof Structure and Dynamicsin a Transiently Populated Protein Folding Intermediate
Enrico Rennella, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge and Bernhard Brutscher
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja302598j/aop/images/medium/ja-2012-02598j_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja302598j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/TMtxa4gIZm4
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05-08-2012 05:37 AM
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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06-29-2011 04:45 AM
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
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Protein Sci. 2011 Feb;20(2):229-46
Authors: Clore GM
Sparsely populated states of macromolecules, characterized by short lifetimes and high free-energies relative to the predominant ground state, often play a key role in many biological, chemical, and biophysical processes. In this review, we briefly summarize various new developments in NMR...
[NMR paper] Two folded conformers of ubiquitin revealed by high-pressure NMR.
Two folded conformers of ubiquitin revealed by high-pressure NMR.
Related Articles Two folded conformers of ubiquitin revealed by high-pressure NMR.
Biochemistry. 2001 Nov 13;40(45):13556-63
Authors: Kitahara R, Yamada H, Akasaka K
High-pressure 15N/1H two-dimensional NMR spectroscopy has been utilized to study conformational fluctuation of a 76-residue protein ubiquitin at pH 4.5 at 20 degrees C. The on-line variable pressure cell technique is used in conjunction with a high-field NMR spectrometer operating at 750 MHz for 1H in the pressure...
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11-19-2010 08:44 PM
[NMR paper] HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structu
HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations.
Related Articles HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations.
J Magn Reson. 2000 Nov;147(1):138-46
Authors: García de la Torre J, Huertas ML, Carrasco B
The heteronuclear NMR relaxation of globular proteins depends on the anisotropic rotational diffusion tensor. Using our previous developments for prediction of hydrodynamic properties of arbitrarily...
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11-19-2010 08:29 PM
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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NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
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