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

Favrin, Giorgio LU ; Irbäck, Anders LU and Wallin, Stefan LU (2004) In Proteins 54(1). p.8-12
Abstract
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.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bundle, Monte Carlo simulation, folding thermodynamics, protein folding, folding kinetics, three-helix, unstructured protein
in
Proteins
volume
54
issue
1
pages
8 - 12
publisher
John Wiley & Sons
external identifiers
  • wos:000187806400002
  • pmid:14705019
  • scopus:0347416919
ISSN
0887-3585
DOI
10.1002/prot.10575
language
English
LU publication?
yes
id
8adc7836-9977-48d5-b826-7f275a44a8de (old id 289951)
date added to LUP
2007-10-22 17:57:26
date last changed
2017-01-01 07:05:40
@article{8adc7836-9977-48d5-b826-7f275a44a8de,
  abstract     = {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.},
  author       = {Favrin, Giorgio and Irbäck, Anders and Wallin, Stefan},
  issn         = {0887-3585},
  keyword      = {bundle,Monte Carlo simulation,folding thermodynamics,protein folding,folding kinetics,three-helix,unstructured protein},
  language     = {eng},
  number       = {1},
  pages        = {8--12},
  publisher    = {John Wiley & Sons},
  series       = {Proteins},
  title        = {Sequence-based study of two related proteins with different folding behaviors},
  url          = {http://dx.doi.org/10.1002/prot.10575},
  volume       = {54},
  year         = {2004},
}