Related ArticlesNMR in a crystallography-based high-throughput protein structure-determination environment.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1365-6
Authors: Wüthrich K
An introduction is provided to three papers which compare corresponding protein crystal and NMR solution structures determined by the Joint Center for Structural Genomics (JCSG). Special mention is made of the JCSG strategy for combined use of the two techniques, and of potential applications of the concept of `reference crystal structures', which is introduced in the following three papers.
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
High-Pressure Protein Crystallography and NMR to Explore Protein Conformations.
Annu Rev Biophys. 2010 Jul 21;
Authors: Collins MD, Kim CU, Gruner SM
High-pressure methods for solving protein structures by X-ray crystallography and NMR are maturing. These techniques are beginning to impact our understanding of thermodynamic and structural features that define not only the protein's native conformation, but also the higher free energy conformations. The ability of...
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[NMR paper] NMR data collection and analysis protocol for high-throughput protein structure determination.
NMR data collection and analysis protocol for high-throughput protein structure determination.
Related Articles NMR data collection and analysis protocol for high-throughput protein structure determination.
Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10487-92
Authors: Liu G, Shen Y, Atreya HS, Parish D, Shao Y, Sukumaran DK, Xiao R, Yee A, Lemak A, Bhattacharya A, Acton TA, Arrowsmith CH, Montelione GT, Szyperski T
A standardized protocol enabling rapid NMR data collection for high-quality protein structure determination is presented that...
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12-01-2010 06:56 PM
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...
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11-25-2010 08:21 PM
[NMR paper] Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignm
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Related Articles Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8009-14
Authors: Szyperski T, Yeh DC, Sukumaran DK, Moseley HN, Montelione GT
A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR experiments is presented for rapid and complete protein resonance assignment. Even when using short measurement times, these experiments allow one to retain...
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11-24-2010 08:49 PM
[NMR paper] An approach for high-throughput structure determination of proteins by NMR spectrosco
An approach for high-throughput structure determination of proteins by NMR spectroscopy.
Related Articles An approach for high-throughput structure determination of proteins by NMR spectroscopy.
J Biomol NMR. 2000 Nov;18(3):229-38
Authors: Medek A, Olejniczak ET, Meadows RP, Fesik SW
An approach is described for rapidly determining protein structures by NMR that utilizes proteins containing 13C-methyl labeled Val, Leu, and Ile (delta1) and protonated Phe and Tyr in a deuterated background. Using this strategy, the key NOEs that define the...
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11-19-2010 08:29 PM
[NMR paper] NMR and crystallography--complementary approaches to structure determination.
NMR and crystallography--complementary approaches to structure determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and crystallography--complementary approaches to structure determination.
Trends Biotechnol. 1994 May;12(5):149-53
Authors: MacArthur MW, Driscoll PC, Thornton JM
A knowledge of the three-dimensional structure of a protein is essential to understand how a protein performs its functions. It is also a prime requirement for the rational design...
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08-22-2010 03:33 AM
[NMR paper] NMR and crystallography--complementary approaches to structure determination.
NMR and crystallography--complementary approaches to structure determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and crystallography--complementary approaches to structure determination.
Trends Biotechnol. 1994 May;12(5):149-53
Authors: MacArthur MW, Driscoll PC, Thornton JM
A knowledge of the three-dimensional structure of a protein is essential to understand how a protein performs its functions. It is also a prime requirement for the rational design...
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08-22-2010 03:33 AM
PCS-based structure determination of proteinâ??protein complexes
Abstract A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and 1HN/15N chemical shift perturbation is presented. PCS is induced by a paramagnetic lanthanide ion that is attached to a target protein using a lanthanide binding peptide tag anchored at two points. PCS provides long-range (~40 Ã?) distance and angular restraints between the lanthanide ion and the observed nuclei, while the 1HN/15N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure...
NMR in a crystallography-based high-throughput protein structure-determination enviro
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