Thermodynamics of α- and β-structure formation in proteins
(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:
https://lup.lub.lu.se/record/302323
- author
- Irbäck, Anders LU ; Samuelsson, Björn LU ; Sjunnesson, Fredrik LU and Wallin, Stefan LU
- organization
- publishing date
- 2003
- 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}}, }