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Anders Irbäck and Sandipan Mohanty
Folding Thermodynamics of Peptides
Biophysical Journal 88, 1560-1569
(2005)
Abstract
A simplified interaction potential for protein folding
studies at the atomic level is discussed and tested on a
set of peptides with about 20 residues each. The test set
contains both α-helical (Trp cage, Fs) and
β-sheet (GB1p, GB1m2, GB1m3, Betanova, LLM)
peptides. The model, which is entirely sequence-based, is
able to fold these different peptides for one and the
same choice of model parameters. Furthermore, the melting
behavior of the peptides is in good quantitative
agreement with experimental data. Apparent folded
populations obtained using different observables are
compared, and are found to be very different for some of
the peptides (e.g., Betanova). In other cases (in
particular, GB1m2 and GB1m3), the different estimates
agree reasonably well, indicating a more two-state-like
melting behavior.
LU TP 04-28
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