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.

• Författare: Anders Irbäck; Björn Samuelsson; Fredrik Sjunnesson; Stefan Wallin
• Avdelning/ar: Beräkningsbiologi och biologisk fysik - Genomgår omorganisation
• Publiceringsår: 2003
• Språk: Engelska
• Sidor: 1466-1473
• Publikation/Tidskrift/Serie: Biophysical Journal
• Volym: 85
• Issue: 3
• Länkar: http://www.biophysj.org/cgi/content/abstract/85/3/1466
• Dokumenttyp: Artikel i tidskrift
• Förlag: Cell Press
• Ämne: Biophysics
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 1542-0086