Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Thermodynamics of α- and β-structure formation in proteins

Irbäck, Anders LU orcid ; Samuelsson, Björn LU ; Sjunnesson, Fredrik LU and Wallin, Stefan LU (2003) In Biophysical Journal 85(3). p.1466-1473
Abstract
An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biophysical Journal
volume
85
issue
3
pages
1466 - 1473
publisher
Cell Press
external identifiers
  • wos:000185009900011
  • scopus:0041629626
ISSN
1542-0086
language
English
LU publication?
yes
id
8c37fa54-34da-4953-a4e2-500a763807a9 (old id 302323)
alternative location
http://www.biophysj.org/cgi/content/abstract/85/3/1466
date added to LUP
2016-04-01 11:37:30
date last changed
2024-02-22 23:03:43
@article{8c37fa54-34da-4953-a4e2-500a763807a9,
  abstract     = {{An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.}},
  author       = {{Irbäck, Anders and Samuelsson, Björn and Sjunnesson, Fredrik and Wallin, Stefan}},
  issn         = {{1542-0086}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{1466--1473}},
  publisher    = {{Cell Press}},
  series       = {{Biophysical Journal}},
  title        = {{Thermodynamics of α- and β-structure formation in proteins}},
  url          = {{http://www.biophysj.org/cgi/content/abstract/85/3/1466}},
  volume       = {{85}},
  year         = {{2003}},
}