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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Jul 1;90(13):6365–6368. doi: 10.1073/pnas.90.13.6365

Kinematics and thermodynamics of a folding heteropolymer.

M Fukugita 1, D Lancaster 1, M G Mitchard 1
PMCID: PMC46929  PMID: 8327518

Abstract

In order to elucidate the folding dynamics of protein, we have carried out numerical simulations of a heteropolymer model of self-interacting random chains. We find that folding propensity depends strongly on sequence and that both folding and nonfolding sequences exist. Furthermore we show that folding is a two-step process: the transition from coil state to unique folded state takes place through a globule phase. In addition to the continuous coil-globule transition, there exists an abrupt transition that separates the unique folded state from the globule state and ensures the stability of the native state.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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