NMR studies of protein structure and dynamics - A look backwards and forwards.
J Magn Reson. 2011 Aug 30;
Authors: Kay LE
Abstract
NMR spectroscopy has evolved to become one of the most powerful tools for the study of protein structure and dynamics. Advances over the past decade have greatly extended the methodology to studies of molecules of ever increasing complexity. Herein I provide a short perspective relating the circumstances that led to some of the contributions from my laboratory in this area and highlight how these original experiments, summarized in a Journal of Magnetic Resonance article in 2005 (JMR, 173 193-207), have influenced the current focus of my research.
PMID: 21885309 [PubMed - as supplied by publisher]
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
NMR studies of protein structure and dynamics – A look backwards and forwards
NMR studies of protein structure and dynamics – A look backwards and forwards
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 31 August 2011</br>
Lewis E., Kay</br>
NMR spectroscopy has evolved to become one of the most powerful tools for the study of protein structure and dynamics. Advances over the past decade have greatly extended the methodology to studies of molecules of ever increasing complexity. Herein I provide a short perspective relating the circumstances that led to some of the contributions from my laboratory in...
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08-31-2011 07:12 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
[NMR paper] NMR studies of protein structure and dynamics.
NMR studies of protein structure and dynamics.
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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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Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
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The structure and dynamics of the R6 human insulin hexamer are investigated by two- and three-dimensional homonuclear 1H-NMR spectroscopy....
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[NMR paper] NMR studies of structure and dynamics of isotope enriched proteins.
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Authors: Wagner G, Thanabal V, Stockman BJ, Peng JW, Nirmala NR, Hyberts SG, Goldberg MS, Detlefsen DJ, Clubb RT, Adler M
Structural studies of globular proteins by nmr can be enhanced by the use of isotope enrichment. We have been working with proteins enriched with 15N, and with both 15N and 13C. Due to the isotope enrichment we could assign several large...
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08-21-2010 11:41 PM
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Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....