Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Folding of a small helical protein using hydrogen bonds and hydrophobicity forces.

Författare

Summary, in English

A reduced protein model with five to six atoms per amino acid and five amino acid types is developed and tested on a three-helix-bundle protein, a 46-amino acid fragment from staphylococcal protein A. The model does not rely on the widely used Go approximation, which ignores non-native interactions. We find that the collapse transition is considerably more abrupt for the protein A sequence than for random sequences with the same composition. The chain collapse is found to be at least as fast as helix formation. Energy minimization restricted to the thermodynamically favored topology gives a structure that has a root-mean-square deviation of 1.8 A from the native structure. The sequence-dependent part of our potential is pairwise additive. Our calculations suggest that fine-tuning this potential by parameter optimization is of limited use.

Publiceringsår

2002

Språk

Engelska

Sidor

99-105

Publikation/Tidskrift/Serie

Proteins

Volym

47

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

John Wiley & Sons Inc.

Ämne

  • Biophysics

Nyckelord

  • Hydrophobicity
  • Models
  • Molecular
  • Molecular Sequence Data
  • Monte Carlo Method
  • Peptide Fragments : chemistry
  • Protein Folding
  • Protein Structure
  • Proteins : chemistry
  • Staphylococcal Protein A : chemistry
  • Secondary
  • Kinetics
  • Support
  • Non-U.S. Gov't
  • Hydrogen Bonding
  • Amino Acid Sequence
  • Comparative Study

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0887-3585