Related ArticlesYoung Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR.
Protein Sci. 1994 Mar;3(3):372-90
Authors: Clore GM, Gronenborn AM
The recent development of a whole panoply of multidimensional heteronuclear-edited and -filtered NMR experiments has revolutionized the field of protein structure determination by NMR, making it possible to extend the methodology from the 10-kDa limit of conventional 2-dimensional NMR to systems up to potentially 35-40 kDa. The basic strategy for solving 3-dimensional structures of larger proteins and protein-ligand complexes in solution using 3- and 4-dimensional NMR spectroscopy is summarized, and the power of these methods is illustrated using 3 examples: interleukin-1 beta, the complex of calmodulin with a target peptide, and the specific complex of the transcription factor GATA-1 with its cognate DNA target site.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
J Am Chem Soc. 2010 Dec 16;
Authors: Gossert AD, Hiller S, Ferna?ndez C
The detection and structural characterization of protein-ligand interactions by solution NMR is central to functional biology research as well as to drug discovery. Here we present a robust and highly automated procedure for obtaining the resonance assignments necessary for studies of such...
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[NMR paper] NMR structure determination of proteins and protein complexes larger than 20 kDa.
NMR structure determination of proteins and protein complexes larger than 20 kDa.
Related Articles NMR structure determination of proteins and protein complexes larger than 20 kDa.
Curr Opin Chem Biol. 1998 Oct;2(5):564-70
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional nuclear magnetic resonance methodology to obtain 1H, 15N and 13C resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long-range order, coupled with new methods of structure refinement and novel methods...
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[NMR paper] An approach to global fold determination using limited NMR data from larger proteins
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
J Biomol NMR. 1996 Oct;8(3):360-8
Authors: Smith BO, Ito Y, Raine A, Teichmann S, Ben-Tovim L, Nietlispach D, Broadhurst RW, Terada T, Kelly M, Oschkinat H, Shibata T, Yokoyama S, Laue ED
A combination of calculation and experiment is used to demonstrate that the global fold of...
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[NMR paper] Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and p
Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR.
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[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dime
Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Related Articles Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.
Prog Biophys Mol Biol. 1994;62(2):153-84
Authors: Clore GM, Gronenborn AM
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[NMR paper] 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 k
1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
Int J Biol Macromol. 1994 Oct;16(5):227-35
Authors: Gettins PG
The three-dimensional solution structures of proteins larger than about 25 kDa cannot at present be determined by multi-dimensional nuclear magnetic resonance (NMR) methods. However,...
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[NMR paper] Structures of larger proteins in solution: three- and four-dimensional heteronuclear
Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
Related Articles Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy.
Science. 1991 Jun 7;252(5011):1390-9
Authors: Clore GM, Gronenborn AM
Three- and four-dimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy offers dramatic improvements in spectral resolution by spreading through-bond and through-space correlations in three and four orthogonal frequency axes....
Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and p
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