Related ArticlesValidating the use of database potentials in protein structure determination by NMR.
FEBS Lett. 2005 Oct 24;579(25):5542-8
Authors: Mertens HD, Gooley PR
The refinement of protein structures determined by nuclear magnetic resonance spectroscopy against database potentials of mean force allows for the exclusion of unfavourable conformations of the protein backbone during a structure calculation, resulting in protein structures with a marked improvement in Ramachandran statistics. In this communication, we use multiple sets of residual dipolar couplings as quality assessment criteria for several proteins and show that not only do the Ramachandran and structural quality statistics improve, but a significant improvement in the accuracy of structures is achieved upon refinement.
DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release)
DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release)
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DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking
7thSpace Interactive (press release)
Unfortunately, the experimental determination of protein-RNA complexes is tedious and difficult, both by X-ray crystallography and NMR. For many interacting proteins and RNAs the individual structures are available, enabling computational prediction of ...
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08-19-2011 04:02 AM
Searching the protein structure database for ligand-binding site similarities ... - 7thSpace Interactive (press release)
Searching the protein structure database for ligand-binding site similarities ... - 7thSpace Interactive (press release)
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Searching the protein structure database for ligand-binding site similarities ...
7thSpace Interactive (press release)
CPASS is an important component of our Functional Annotation Screening Technology by NMR (FAST-NMR) protocol and has been successfully applied to aid the ...
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Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Related Articles Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
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12-08-2010 06:21 PM
[NMR paper] Relationships between protein structure and dynamics from a database of NMR-derived b
Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
Related Articles Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
J Mol Biol. 2000 Jan 28;295(4):963-78
Authors: Goodman JL, Pagel MD, Stone MJ
The amplitude of protein backbone NH group motions on a time-scale faster than molecular tumbling may be determined by analysis of (15)N NMR relaxation data according to the Lipari-Szabo model free formalism. An internet-accessible...
NMR-Based Protein Potentials.
NMR-Based Protein Potentials.
Related Articles NMR-Based Protein Potentials.
Angew Chem Int Ed Engl. 2010 Aug 16;
Authors: Li DW, Brüschweiler R
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08-18-2010 11:15 AM
A probabilistic approach for validating protein NMR chemical shift assignments
Abstract It has been estimated that more than 20% of the proteins in the BMRB are improperly referenced and that about 1% of all chemical shift assignments are mis-assigned. These statistics also reflect the likelihood that any newly assigned protein will have shift assignment or shift referencing errors. The relatively high frequency of these errors continues to be a concern for the biomolecular NMR community. While several programs do exist to detect and/or correct chemical shift mis-referencing or chemical shift mis-assignments, most can only do one, or the other. The one program...
Validating the use of database potentials in protein structure determination by NMR.
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