Sequence-based study of two related proteins with different folding behaviors
(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:
https://lup.lub.lu.se/record/289951
- author
- Favrin, Giorgio LU ; Irbäck, Anders LU and Wallin, Stefan LU
- organization
- publishing date
- 2004
- 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 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
- 2024-01-11 08:20:16
@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 = {{John Wiley & Sons 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}}, }