Related ArticlesEvaluation of the utility of NMR structures determined from minimal NOE-based restraints for structure-based drug design, using MMP-1 as an example.
Biochemistry. 2000 Nov 7;39(44):13365-75
Authors: Huang X, Moy F, Powers R
The application of deuterium labeling and residual dipolar coupling constants in combination with other structural information has demonstrated the potential for significantly expanding the range of viable protein targets for structural analysis by NMR. A previous study by Clore et al. [(1999) J. Am. Chem. Soc. 121, 6513-6514] demonstrated that a significant improvement in the overall protein structure occurs with the combination of residual dipolar coupling constants and minimal tertiary long-range distance restraints. The analysis of NMR protein structures determined with minimal structural information is extended with a particular interest in the utility of these structures for a structure-based drug design program. As an example, the catalytic fragment of human fibroblast collagenase (MMP-1) was used to follow the effect of minimal restraint sets on the protein structure and its utility in drug design with a particular interest in the effect on the active site conformation. An MMP-1 structure that was calculated with the maximal number of restraints attainable with the constraint of a deuterated protein was shown to be very similar to a high-quality MMP-1 structure that was calculated from a complete set of restraints. The superposition of the active site backbone atoms for the high-quality and minimal restraint MMP-1 structures yielded an rmsd of 0.68 A where the size and shape of the S1' pocket are nearly identical. Additionally, an MMP-1-CGS-27023A complex based on a minimal set of NOE-based restraints reliably reproduced the structure of the complex, establishing the usefulness of the structures for drug design.
[KPWU blog] statistics of NMR/X-ray determined protein structures in PDB (up to May 10, 2011)
statistics of NMR/X-ray determined protein structures in PDB (up to May 10, 2011)
Two brief plots of protein structures (protein-DNA/RNA/ligand complexes are excluded) determined by either X-ray or NMR. Structures determined by hybrid method are not counted in the two plots. The dataset was obtain from PDB based on its released statistics by May 10th, 2011. Molecules with sequence length longer than 1200 residues are also excluded. There http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=380&subd=kpwu&ref=&feed=1
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[NMR paper] Relative stability of protein structures determined by X-ray crystallography or NMR s
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
Related Articles Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
Proteins. 2003 Oct 1;53(1):111-20
Authors: Fan H, Mark AE
The relative stability of protein structures determined by either X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy has been investigated by using molecular dynamics simulation...
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11-24-2010 09:16 PM
[NMR paper] An assessment of the precision and accuracy of protein structures determined by NMR.
An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
J Mol Biol. 1994 Jun 24;239(5):601-7
Authors: Zhao D, Jardetzky O
We tested the dependence of the accuracy and precision of calculated NMR structures on the errors of the distance constraints...
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08-22-2010 03:33 AM
[NMR paper] An assessment of the precision and accuracy of protein structures determined by NMR.
An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
J Mol Biol. 1994 Jun 24;239(5):601-7
Authors: Zhao D, Jardetzky O
We tested the dependence of the accuracy and precision of calculated NMR structures on the errors of the distance constraints...
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08-22-2010 03:33 AM
[NMR paper] SESAME: a least-squares approach to the evaluation of protein structures computed fro
SESAME: a least-squares approach to the evaluation of protein structures computed from NMR data.
Related Articles SESAME: a least-squares approach to the evaluation of protein structures computed from NMR data.
J Biomol NMR. 1993 May;3(3):355-60
Authors: Yang JX, Havel TF
A method is proposed for defining a probability distribution on an ensemble of protein conformations from a 2D NOE spectrum, while at the same time back-calculating the experimental spectrum from the ensemble. This enables one to assess the relative quality and significance...
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08-21-2010 11:53 PM
[NMR paper] Comparison of protein structures determined by NMR in solution and by X-ray diffracti
Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
Related Articles Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
Q Rev Biophys. 1992 Aug;25(3):325-77
Authors: Billeter M
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Major groove width variations in RNA structures determined by NMR and impact of 13C r
Abstract Ribonucleic acid structure determination by NMR spectroscopy relies primarily on local structural restraints provided by 1Hâ?? 1H NOEs and J-couplings. When employed loosely, these restraints are broadly compatible with A- and B-like helical geometries and give rise to calculated structures that are highly sensitive to the force fields employed during refinement. A survey of recently reported NMR structures reveals significant variations in helical parameters, particularly the major groove width. Although helical parameters observed in high-resolution X-ray crystal structures of...
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08-14-2010 04:19 AM
Investigation of the utility of selective methyl protonation for determination of membrane protein structures
Investigation of the utility of selective methyl protonation for determination of membrane protein structures
Steve C. C. Shih, Ileana Stoica and Natalie K. Goto
Journal of Biomolecular NMR; 2008; 42(1); pp 49-58
Abstract
Polytopic α-helical membrane proteins present one of the final frontiers for protein structural biology, with significant challenges causing severe under-representation in the protein structure databank. However, with the advent of hardware and methodology geared to the study of large molecular weight complexes, solution NMR is being increasingly considered as a tool...
Evaluation of the utility of NMR structures determined from minimal NOE-based restrai
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