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Sequence-based study of two related proteins with different folding behaviors

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Author

Summary, in English

Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. (C) 2003 Wiley-Liss, Inc.

Publishing year

2004

Language

English

Pages

8-12

Publication/Series

Proteins

Volume

54

Issue

1

Document type

Journal article

Publisher

John Wiley & Sons Inc.

Topic

  • Biophysics

Keywords

  • bundle
  • Monte Carlo simulation
  • folding thermodynamics
  • protein folding
  • folding kinetics
  • three-helix
  • unstructured protein

Status

Published

ISBN/ISSN/Other

  • ISSN: 0887-3585