Thermodynamics of α- and β-structure formation in proteins

Summary, in English

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 Irbäck; Björn Samuelsson; Fredrik Sjunnesson; Stefan Wallin
• Department/s: Computational Biology and Biological Physics - Undergoing reorganization
• Publishing year: 2003
• Language: English
• Pages: 1466-1473
• Publication/Series: Biophysical Journal
• Volume: 85
• Issue: 3
• Links: http://www.biophysj.org/cgi/content/abstract/85/3/1466
• Document type: Journal article
• Publisher: Cell Press
• Topic: Biophysics
• Status: Published
• ISBN/ISSN/Other: ISSN: 1542-0086