Journal of Biomolecular NMR

, Volume 18, Issue 1, pp 43–48 | Cite as

Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView

  • Stephan Schwarzinger
  • Gerard J.A. Kroon
  • Ted R. Foss
  • Peter E. Wright
  • H. Jane Dyson
Article

Abstract

Studies of proteins unfolded in acid or chemical denaturant can help in unraveling events during the earliest phases of protein folding. In order for meaningful comparisons to be made of residual structure in unfolded states, it is necessary to use random coil chemical shifts that are valid for the experimental system under study. We present a set of random coil chemical shifts obtained for model peptides under experimental conditions used in studies of denatured proteins. This new set, together with previously published data sets, has been incorporated into a software interface for NMRView, allowing selection of the random coil data set that fits the experimental conditions best.

chemical shift CSI denaturant NMRView peptide random coil 

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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Stephan Schwarzinger
    • 1
  • Gerard J.A. Kroon
    • 1
  • Ted R. Foss
    • 1
  • Peter E. Wright
    • 1
  • H. Jane Dyson
    • 1
  1. 1.Department of Molecular Biology and Skaggs Institute for Chemical BiologyThe Scripps Research InstituteLa JollaU.S.A.

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