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

Favrin, Giorgio LU ; Irbäck, Anders LU orcid 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
; and
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
Wiley-Liss Inc.
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
2016-04-01 16:27:05
date last changed
2025-10-14 11:25:49
@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}},
  keywords     = {{bundle; Monte Carlo simulation; folding thermodynamics; protein folding; folding kinetics; three-helix; unstructured protein}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{8--12}},
  publisher    = {{Wiley-Liss Inc.}},
  series       = {{Proteins}},
  title        = {{Sequence-based study of two related proteins with different folding behaviors}},
  url          = {{http://dx.doi.org/10.1002/prot.10575}},
  doi          = {{10.1002/prot.10575}},
  volume       = {{54}},
  year         = {{2004}},
}