Thermodynamics of α- and β-structure formation in proteins

Research output: Contribution to journalArticle

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.

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Subject classification (UKÄ) – MANDATORY

  • Biophysics
Original languageEnglish
Pages (from-to)1466-1473
JournalBiophysical Journal
Volume85
Issue number3
Publication statusPublished - 2003
Publication categoryResearch
Peer-reviewedYes

Related research output

Wallin, S., 2003, Department of Theoretical Physics, Lund University. 160 p.

Research output: ThesisDoctoral Thesis (compilation)

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