Thermodynamics of α- and β-structure formation in proteins
Forskningsoutput: Tidskriftsbidrag › Artikel i vetenskaplig tidskrift
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.
Detaljer
Författare | |
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Enheter & grupper | |
Forskningsområden | Ämnesklassifikation (UKÄ) – OBLIGATORISK
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Originalspråk | engelska |
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Sidor (från-till) | 1466-1473 |
Tidskrift | Biophysical Journal |
Volym | 85 |
Utgåva nummer | 3 |
Status | Published - 2003 |
Publikationskategori | Forskning |
Peer review utförd | Ja |
Relaterad forskningsoutput
Stefan Wallin, 2003, Department of Theoretical Physics, Lund University. 160 s.
Forskningsoutput: Avhandling › Doktorsavhandling (sammanläggning)