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[Question from NMRWiki Q&A forum] How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
Dear Friends
we have done HSQC gradient titration with targeted proteins , most of cross peaks we observed intensity drop , 30 out of 95 peaks ( 70 percent intensity drop of each cross peak ) , other cross peaks also we observe intensity drop less than 70 percent , we did n"t observe any chemical shift change .( May be it is due to intermediate exchange regime of complex ) .ITC experiment showing 12uM binding constant .AUC experiment result is...
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05-09-2012 07:38 PM
RefDB: Re-referenced Protein Chemical Shift Database
RefDB website
In case of the BMRB, it is known that a significant portion of depositions use different or non-IUPAC chemical shift reference standards. This lack of uniformity makes it difficult to extract sequence/structure relationships from chemical shifts. Nearly 40% of protein entries deposited in the BioMagResBank appear to have at least one assignment error. In addition, it evident that protein NMR spectroscopists are increasingly adhering to recommended IUPAC (13)C and (15)N chemical shift referencing conventions, however, approximately 20% of newly deposited protein entries in the...
[NMR paper] Validating the use of database potentials in protein structure determination by NMR.
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FEBS Lett. 2005 Oct 24;579(25):5542-8
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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...
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12-01-2010 06:56 PM
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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...
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[NMR paper] Comparison between the phi distribution of the amino acids in the protein database an
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
J Mol Biol. 1995 Nov 24;254(2):322-33
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08-22-2010 03:50 AM
[NMR paper] A relational database for sequence-specific protein NMR data.
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J Biomol NMR. 1991 Sep;1(3):217-36
Authors: Seavey BR, Farr EA, Westler WM, Markley JL
A protein NMR database has been designed and is being implemented. The database is intended to contain solution NMR results from proteins and peptides (larger than 12 residues). A relational database format has been chosen that indexes data by: primary journal citation, molecular species, sequence-related and...
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08-21-2010 11:12 PM
[NMR paper] A relational database for sequence-specific protein NMR data.
A relational database for sequence-specific protein NMR data.
Related Articles A relational database for sequence-specific protein NMR data.
J Biomol NMR. 1991 Sep;1(3):217-36
Authors: Seavey BR, Farr EA, Westler WM, Markley JL
A protein NMR database has been designed and is being implemented. The database is intended to contain solution NMR results from proteins and peptides (larger than 12 residues). A relational database format has been chosen that indexes data by: primary journal citation, molecular species, sequence-related and...
Welcome to the protein NMR pH titration database.
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