Related ArticlesStructure 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 linkages. Significant progress has been made possible by dramatic improvements in NMR techniques and advances in computational chemistry and technology. Transferred nuclear Overhauser effects have been used to infer the conformations of carbohydrate ligands bound to protein receptors such as antibodies, lectins and enzymes. The increased use of combined NMR spectroscopic and computational protocols has resulted in insights into the dynamics of glycan chains.
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.
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
[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] NMR structure of the extended Myb cognate sequence and modeling studies on specific D
NMR structure of the extended Myb cognate sequence and modeling studies on specific DNA-Myb complexes.
Related Articles NMR structure of the extended Myb cognate sequence and modeling studies on specific DNA-Myb complexes.
Biochemistry. 1998 Jul 14;37(28):9952-63
Authors: Radha PK, Patel PK, Hosur RV
The recognition sequence of the Myb protein has been recently described to be pyAACKGHH (where py = T/C, K = G/T, and H = A/C/T), modifying the earlier identification as pyAACKG . We had earlier determined the solution structure of the minimal...
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11-17-2010 11:15 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] NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif Related Articles NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.
Glycobiology. 1999 Jul;9(7):669-77
Authors: Agrawal PK, Jacquinet JC, Krishna NR
Complete 1H and 13C NMR...
Structure and dynamics of oligosaccharides: NMR and modeling studies.
Linear Mode
