Improved chemical shift prediction by Rosetta conformational sampling. J Biomol NMR 2012 Nov;54(3):237-43
Date
09/26/2012Pubmed ID
23007199Pubmed Central ID
PMC3484222DOI
10.1007/s10858-012-9677-7Scopus ID
2-s2.0-84868205509 (requires institutional sign-in at Scopus site) 6 CitationsAbstract
Chemical shift frequencies represent a time-average of all the conformational states populated by a protein. Thus, chemical shift prediction programs based on sequence and database analysis yield higher accuracy for rigid rather than flexible protein segments. Here we show that the prediction accuracy can be significantly improved by averaging over an ensemble of structures, predicted solely from amino acid sequence with the Rosetta program. This approach to chemical shift and structure prediction has the potential to be useful for guiding resonance assignments, especially in solid-state NMR structural studies of membrane proteins in proteoliposomes.
Author List
Tian Y, Opella SJ, Marassi FMAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceMembrane Proteins
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Proteins
Software
