Coexistence of Native and Denatured Phases in a Single Proteinlike Molecule

Rose Du, Alexander Yu Grosberg, Toyoichi Tanaka

    Research output: Contribution to journalArticle

    Abstract

    In order to understand the nuclei which develop during the course of protein folding and unfolding, we examine equilibrium coexistence of phases within a single heteropolymer chain. We computationally generate the phase segregation by applying a "folding pressure," or adding an energetic bonus for native monomer-monomer contacts. The computer models reveal that in a polymer system some nuclei hinder folding via topological constraints. Using this insight, we show that the critical nucleus size is of the order of the entire chain and that unfolding time scales as exp(cN2/3), in the large N limit, N and c being the chain length and a constant, respectively.

    Original languageEnglish (US)
    Pages (from-to)4670-4673
    Number of pages4
    JournalPhysical Review Letters
    Volume83
    Issue number22
    StatePublished - Nov 29 1999

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    folding
    nuclei
    monomers
    molecules
    proteins
    polymers

    ASJC Scopus subject areas

    • Physics and Astronomy(all)

    Cite this

    Du, R., Grosberg, A. Y., & Tanaka, T. (1999). Coexistence of Native and Denatured Phases in a Single Proteinlike Molecule. Physical Review Letters, 83(22), 4670-4673.

    Coexistence of Native and Denatured Phases in a Single Proteinlike Molecule. / Du, Rose; Grosberg, Alexander Yu; Tanaka, Toyoichi.

    In: Physical Review Letters, Vol. 83, No. 22, 29.11.1999, p. 4670-4673.

    Research output: Contribution to journalArticle

    Du, R, Grosberg, AY & Tanaka, T 1999, 'Coexistence of Native and Denatured Phases in a Single Proteinlike Molecule', Physical Review Letters, vol. 83, no. 22, pp. 4670-4673.
    Du, Rose ; Grosberg, Alexander Yu ; Tanaka, Toyoichi. / Coexistence of Native and Denatured Phases in a Single Proteinlike Molecule. In: Physical Review Letters. 1999 ; Vol. 83, No. 22. pp. 4670-4673.
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