Solution nuclear magnetic resonance (NMR) spectroscopy is unique in its ability to elucidate the details of atomic-level structural and dynamical properties of biological macromolecules under native-like conditions. Recent advances in NMR techniques and protein sample preparation now allow comprehensive investigation of protein dynamics over timescales ranging 14 orders of magnitude at nearly every atomic site. Thus, solution NMR is poised to reveal aspects of the physico-chemical properties that govern the ensemble distribution of protein conformers and the dynamics of their interconversion. We review these advances as well as their recent application to the study of proteins.
Protein NMR - A Practical Guide - Solution NMR Assignment Theory
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Assignment - Theory
The most simple and straight forward method of backbone resonance assignment involves the use of 15N,13C labelled protein and the measurement of CBCANNH and CBCA(CO)NNH spectra.
Large Proteins
Large proteins give worse NMR spectra, because they tumble more slowly. For this reason the CBCANNH and CBCA(CO)NNH spectra of larger proteins (> 150...
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11-06-2011 09:42 PM
A solution NMR view of protein dynamics in the biological membrane.
A solution NMR view of protein dynamics in the biological membrane.
A solution NMR view of protein dynamics in the biological membrane.
Curr Opin Struct Biol. 2011 Jul 30;
Authors: Chill JH, Naider F
Structure determination of membrane-associated proteins (MPs) represents a frontier of structural biology that is characterized by unique challenges in sample preparation and data acquisition. No less important is our ability to study the dynamics of MPs, since MP flexibility and characteristic motions often make sizeable contributions to their...
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08-03-2011 12:00 PM
Current Applications of 19F NMR to Studies of Protein Structure and Dynamics
Current Applications of 19F NMR to Studies of Protein Structure and Dynamics
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 13 July 2011</br>
Julianne L., Kitevski-LeBlanc , R., Scott Prosser</br>
*Highlights:*? 19F molecular tags and labelling protocols for 19F NMR studies of proteins are reviewed and contrasted. ? 19F NMR biosynthetic labelling strategies are presented. ? Experimental challenges (loss of function through labelling, line broadening, assignment ambiguities) are discussed. ?...
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07-14-2011 08:55 PM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supramolecular Protein Systems: Applications to the Proteasome and to the ClpP Protease
Tomasz L. Religa, Amy M. Ruschak, Rina Rosenzweig and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202259a/aop/images/medium/ja-2011-02259a_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202259a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/rQfCMlQFoW8
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05-20-2011 09:17 PM
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
Site-Directed Methyl Group Labeling as an NMR Probe of Structure and Dynamics in Supra-Molecular Protein Systems: Applications to the Proteasome and to the ClpP Protease.
J Am Chem Soc. 2011 May 11;
Authors: Religa TL, Ruschak AM, Rosenzweig R, Kay LE
Methyl groups are powerful reporters of structure, motion and function in NMR studies of supra-molecular protein assemblies. Their...
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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02-08-2011 06:28 PM
NMR Spectroscopy Explained: Simplified Theory, Applications and Examples for Organic Chemistry and Structural Biology - Thomas L. James (2007)
NMR Spectroscopy Explained: Simplified Theory, Applications and Examples for Organic Chemistry and Structural Biology
Edited by Neil E. Jacobsen (2007)
Amazon book description
NMR Spectroscopy Explained : Simplified Theory, Applications and Examples for Organic Chemistry and Structural Biology provides a fresh, practical guide to NMR for both students and practitioners, in a clearly written and non-mathematical format. It gives the reader an intermediate level theoretical basis for understanding laboratory applications, developing concepts gradually within the context of examples and...
Protein dynamics from solution NMR: theory and applications.
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