Thermodynamics of alpha- and beta-structure formation in proteins

Details Thermodynamics of alpha- and beta-structure formation in proteins Thermodynamics of alpha- and beta-structure formation in proteins

2003-12-30

arxiv.org/abs/q-bio/0312045v1

Biophys. J. 85 (2003) 1466-1473

Biology

Quantitative Biology

Biomolecules

18 pages, 4 figures

Scientific paper

10.1016/S0006-3495(03)74579-2

An atomic protein model with a minimalistic potential is developed and then tested on an alpha-helix and a beta-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 alpha-helix forms faster than the beta-hairpin.

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