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- W2161668221 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." @default.
- W2161668221 created "2016-06-24" @default.
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- W2161668221 date "2003-09-01" @default.
- W2161668221 modified "2023-09-28" @default.
- W2161668221 title "Thermodynamics of α- and β-Structure Formation in Proteins" @default.
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- W2161668221 doi "https://doi.org/10.1016/s0006-3495(03)74579-2" @default.
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