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Folding thermodynamics of peptides

Irbäck, Anders LU and Mohanty, Sandipan LU (2005) In Biophysical Journal 88(3). p.1560-1569
Abstract
A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with; 20 residues each. The test set contains both alpha-helical ( Trp cage, F-s) and beta-sheet ( GB1p, GB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely sequence-based, is able to fold these different peptides for one and the same choice of model parameters. Furthermore, the melting behavior of the peptides is in good quantitative agreement with experimental data. Apparent folded populations obtained using different observables are compared, and are found to be very different for some of the peptides ( e. g., Betanova). In other cases ( in particular, GB1m2 and GB1m3), the different estimates... (More)
A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with; 20 residues each. The test set contains both alpha-helical ( Trp cage, F-s) and beta-sheet ( GB1p, GB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely sequence-based, is able to fold these different peptides for one and the same choice of model parameters. Furthermore, the melting behavior of the peptides is in good quantitative agreement with experimental data. Apparent folded populations obtained using different observables are compared, and are found to be very different for some of the peptides ( e. g., Betanova). In other cases ( in particular, GB1m2 and GB1m3), the different estimates agree reasonably well, indicating a more two-state-like melting behavior. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Journal
volume
88
issue
3
pages
1560 - 1569
publisher
Cell Press
external identifiers
  • wos:000227494600008
  • pmid:15613623
  • scopus:21244495332
ISSN
1542-0086
DOI
10.1529/biophysj.104.050427
language
English
LU publication?
yes
id
86c66261-d15b-4e02-8be6-8a73ce6d64d1 (old id 250360)
date added to LUP
2007-08-13 12:52:30
date last changed
2017-06-25 03:39:10
@article{86c66261-d15b-4e02-8be6-8a73ce6d64d1,
  abstract     = {A simplified interaction potential for protein folding studies at the atomic level is discussed and tested on a set of peptides with; 20 residues each. The test set contains both alpha-helical ( Trp cage, F-s) and beta-sheet ( GB1p, GB1m2, GB1m3, Betanova, LLM) peptides. The model, which is entirely sequence-based, is able to fold these different peptides for one and the same choice of model parameters. Furthermore, the melting behavior of the peptides is in good quantitative agreement with experimental data. Apparent folded populations obtained using different observables are compared, and are found to be very different for some of the peptides ( e. g., Betanova). In other cases ( in particular, GB1m2 and GB1m3), the different estimates agree reasonably well, indicating a more two-state-like melting behavior.},
  author       = {Irbäck, Anders and Mohanty, Sandipan},
  issn         = {1542-0086},
  language     = {eng},
  number       = {3},
  pages        = {1560--1569},
  publisher    = {Cell Press},
  series       = {Biophysical Journal},
  title        = {Folding thermodynamics of peptides},
  url          = {http://dx.doi.org/10.1529/biophysj.104.050427},
  volume       = {88},
  year         = {2005},
}