Publication year: 2011 Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 477-491
Lewis E.*Kay
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 malate synthase G, a 723 residue enzyme that has been a focal point of research efforts in my laboratory. Details of the labeling schemes that have been employed and optimal experiments for extraction of structural and dynamics information on this protein are described. NMR studies of protein dynamics, in principle, give insight into the relation between motion and function. A description of deuterium-based spin relaxation methods for the investigation of side chain dynamics is provided. Examples where millisecond (ms) time scale dynamics play an important role and where relaxation dispersion NMR spectroscopy has been particularly informative, including applications involving the membrane enzyme PagP and mutants of the Fyn SH3 domain that fold on a ms time scale, are presented.
NMR studies of protein structure and dynamics - A look backwards and forwards.
NMR studies of protein structure and dynamics - A look backwards and forwards.
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...
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09-03-2011 06:55 PM
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.
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....
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08-22-2010 02:27 PM
[NMR paper] Structure and dynamics of oligosaccharides: NMR and modeling studies.
Structure and dynamics of oligosaccharides: NMR and modeling studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of oligosaccharides: NMR and modeling studies.
Curr Opin Struct Biol. 1996 Oct;6(5):710-20
Authors: Peters T, Pinto BM
Recent advances in the conformational analysis of oligosaccharides have focused on protein-bound oligosaccharides, glycopeptides, and glycoproteins, as well as on the conformational dynamics about glycosidic...
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08-22-2010 02:20 PM
[NMR paper] NMR studies of structure and dynamics of isotope enriched proteins.
NMR studies of structure and dynamics of isotope enriched proteins.
Related Articles NMR studies of structure and dynamics of isotope enriched proteins.
Biopolymers. 1992 Apr;32(4):381-90
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
[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Related Articles NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
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....
NMR studies of protein structure and dynamics
Linear Mode
