Journal of Biomolecular NMR

, Volume 19, Issue 2, pp 153–165

Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and comparisons with other denatured proteins

  • Wolfgang Peti
  • Lorna J. Smith
  • Christina Redfield
  • Harald Schwalbe
Article

DOI: 10.1023/A:1008307323283

Cite this article as:
Peti, W., Smith, L.J., Redfield, C. et al. J Biomol NMR (2001) 19: 153. doi:10.1023/A:1008307323283
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Abstract

Chemical shift assignment is reported for the protein ubiquitin denatured in 8M urea at pH 2. The variations in 15N chemical shifts of three different proteins (ubiquitin, disulfide reduced, carboxymethylated lysozyme, all-Ala-α-lactalbumin), all without disulfides and denatured in 8M urea at pH 2 are compared to `random coil shifts' of small model peptides (Braun et al., 1994) and to the averaged native chemical shifts taken from the BMRB database. Both parameterizations show a remarkable agreement with the averaged measured 15N chemical shifts in the three denatured proteins. Detailed analysis of these experimental 15N chemical shifts provides an estimate of the influence of nearest neighbors and conformational preferences on the chemical shift and provides a direct means to identify non-random structural preferences in denatured proteins.

chemical shifts denatured proteins α-lactalbumin lysozyme random coil resonance assignment triple resonance NMR ubiquitin 

Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • Wolfgang Peti
    • 1
  • Lorna J. Smith
    • 2
  • Christina Redfield
    • 2
  • Harald Schwalbe
    • 3
  1. 1.Institut für Organische ChemieUniversität FrankfurtFrankfurtGermany
  2. 2.New Chemistry LaboratoryOxford Centre of Molecular SciencesOxfordU.K
  3. 3.Department of Chemistry, Francis Bitter Magnet LaboratoryMassachusetts Institute of TechnologyCambridgeU.S.A

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