Internal Dynamics of Aromatic Residues in Subtilisin BPN’ and Subtilisin Carlsberg: Time-Resolved Fluorescence Properties

  • P. M. Bayley
  • S. R. Martin
  • R. W. Wijnaendts van Resandt
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 1)

Abstract

The time-resolved fluorescence anisotropy of the highly quenched single tryptophan residue in subtilisin Carlsberg shows a fast component with rotational correlation time less than 300 ps. The homologous subtilisin BPN’ shows a similar fast component, plus global motion of the whole protein. We conclude that the Trp in subtilisin Carlsberg (and, by analogy, Trp-113 in subtilisin BPN’) shows an internal dynamic process, independent of the rotational diffusion of the molecule.

Keywords

Glycerol Anisotropy Hydrated Tyrosine Tryptophan 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • P. M. Bayley
    • 1
  • S. R. Martin
    • 1
  • R. W. Wijnaendts van Resandt
    • 2
  1. 1.Division of Physical BiochemistryNational Institute for Medical ResearchMill Hill, LondonUK
  2. 2.European Molecular Biology LaboratoryHeidelbergGermany

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