April 2012
Publication year: 2012 Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 62
Highlights
? 19F molecular tags and labeling protocols for 19F NMR studies of proteins are reviewed and contrasted. ? 19F NMR biosynthetic labeling strategies are presented. ? Experimental challenges (loss of function through labeling, line broadening, assignment ambiguities) are discussed. ? Approaches to the study of protein topology, using 19F NMR, are presented. ? Current examples of protein NMR studies are given.
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: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 62</br>
Julianne L. Kitevski-LeBlanc, R. Scott Prosser</br>
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03-09-2012 09:16 AM
NMR studies of protein structure and dynamics
NMR studies of protein structure and dynamics
Publication year: 2011
Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 477-491</br>
Lewis E.*Kay</br>
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100*kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is provided in a study of...
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12-11-2011 07:57 AM
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...
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05-12-2011 03:40 PM
[NMR paper] NMR studies of protein structure and dynamics.
NMR studies of protein structure and dynamics.
Related Articles NMR studies of protein structure and dynamics.
J Magn Reson. 2005 Apr;173(2):193-207
Authors: Kay LE
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100 kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is...
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11-25-2010 08:21 PM
[NMR paper] Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin
Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
J Mol Biol. 1996 Apr 26;258(1):136-57
Authors: Jacoby E, Hua QX, Stern AS, Frank BH, Weiss MA
The structure and dynamics of the R6 human insulin hexamer are investigated by two- and three-dimensional homonuclear 1H-NMR spectroscopy....
Current applications of 19F NMR to studies of protein structure and dynamics
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