Journal of Biomolecular NMR

, Volume 54, Issue 3, pp 237–243

Improved chemical shift prediction by Rosetta conformational sampling

  • Ye Tian
  • Stanley J. Opella
  • Francesca M. Marassi
Communication

DOI: 10.1007/s10858-012-9677-7

Cite this article as:
Tian, Y., Opella, S.J. & Marassi, F.M. J Biomol NMR (2012) 54: 237. doi:10.1007/s10858-012-9677-7

Abstract

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.

Keywords

Chemical shift Prediction Rosetta Ensemble averaging Structure Membrane protein Solid-state NMR Conformational ensemble 

Copyright information

© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  • Ye Tian
    • 1
    • 2
  • Stanley J. Opella
    • 2
  • Francesca M. Marassi
    • 1
  1. 1.Sanford Burnham Medical Research InstituteLa JollaUSA
  2. 2.Department of Chemistry and BiochemistryUniversity of California San DiegoLa JollaUSA

Personalised recommendations