Thermodynamics of α- and β-structure formation in proteins

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Bibtex

@article{8c37fa5434da4953a4e2500a763807a9,
title = "Thermodynamics of α- and β-structure formation in proteins",
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 = "Anders Irb{\"a}ck and Bj{\"o}rn Samuelsson and Fredrik Sjunnesson and Stefan Wallin",
year = "2003",
language = "English",
volume = "85",
pages = "1466--1473",
journal = "Biophysical Journal",
issn = "1542-0086",
publisher = "Cell Press",
number = "3",

}