期刊
PHYSICAL REVIEW LETTERS
卷 88, 期 25, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.88.258101
关键词
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A transfer-matrix formalism is introduced to evaluate exactly the partition function of the Munoz-Eaton model, relating the folding kinetics of proteins of known structure to their thermodynamics and topology. This technique can be used for a generic protein, for any choice of the energy and entropy parameters, and in principle allows the model to be used as a first tool to characterize the dynamics of a protein of known native state and equilibrium population. Applications to a beta-hairpin and to protein CI-2, with comparisons to previous results, are also shown.
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