Freezing transition of compact polyampholytes

Vijay S. Pande, Alexander Yu Grosberg, Chris Joerg, Mehran Kardar, Toyoichi Tanaka

    Research output: Contribution to journalArticle

    Abstract

    Polyampholytes (PAs) are heteropolymers with long range Coulomb interactions. Unlike polymers with short range forces, PA energy levels have nonvanishing correlations and are thus very different from the random energy model (REM). Nevertheless, if charges in the PA globule are screened as in a regular plasma, PAs freeze in REM fashion. Our results shed light on the potential role of Coulomb interactions in folding and evolution of proteins, which are weakly charged PAs, in particular, making connection with the finding that sequences of charged amino acids in proteins are not random.

    Original languageEnglish (US)
    Pages (from-to)3565-3568
    Number of pages4
    JournalPhysical Review Letters
    Volume77
    Issue number17
    StatePublished - 1996

    Fingerprint

    freezing
    proteins
    globules
    folding
    amino acids
    energy levels
    interactions
    energy
    polymers

    ASJC Scopus subject areas

    • Physics and Astronomy(all)

    Cite this

    Pande, V. S., Grosberg, A. Y., Joerg, C., Kardar, M., & Tanaka, T. (1996). Freezing transition of compact polyampholytes. Physical Review Letters, 77(17), 3565-3568.

    Freezing transition of compact polyampholytes. / Pande, Vijay S.; Grosberg, Alexander Yu; Joerg, Chris; Kardar, Mehran; Tanaka, Toyoichi.

    In: Physical Review Letters, Vol. 77, No. 17, 1996, p. 3565-3568.

    Research output: Contribution to journalArticle

    Pande, VS, Grosberg, AY, Joerg, C, Kardar, M & Tanaka, T 1996, 'Freezing transition of compact polyampholytes', Physical Review Letters, vol. 77, no. 17, pp. 3565-3568.
    Pande VS, Grosberg AY, Joerg C, Kardar M, Tanaka T. Freezing transition of compact polyampholytes. Physical Review Letters. 1996;77(17):3565-3568.
    Pande, Vijay S. ; Grosberg, Alexander Yu ; Joerg, Chris ; Kardar, Mehran ; Tanaka, Toyoichi. / Freezing transition of compact polyampholytes. In: Physical Review Letters. 1996 ; Vol. 77, No. 17. pp. 3565-3568.
    @article{d7e15a88f30f4fdbb4824686dde5ad1a,
    title = "Freezing transition of compact polyampholytes",
    abstract = "Polyampholytes (PAs) are heteropolymers with long range Coulomb interactions. Unlike polymers with short range forces, PA energy levels have nonvanishing correlations and are thus very different from the random energy model (REM). Nevertheless, if charges in the PA globule are screened as in a regular plasma, PAs freeze in REM fashion. Our results shed light on the potential role of Coulomb interactions in folding and evolution of proteins, which are weakly charged PAs, in particular, making connection with the finding that sequences of charged amino acids in proteins are not random.",
    author = "Pande, {Vijay S.} and Grosberg, {Alexander Yu} and Chris Joerg and Mehran Kardar and Toyoichi Tanaka",
    year = "1996",
    language = "English (US)",
    volume = "77",
    pages = "3565--3568",
    journal = "Physical Review Letters",
    issn = "0031-9007",
    publisher = "American Physical Society",
    number = "17",

    }

    TY - JOUR

    T1 - Freezing transition of compact polyampholytes

    AU - Pande, Vijay S.

    AU - Grosberg, Alexander Yu

    AU - Joerg, Chris

    AU - Kardar, Mehran

    AU - Tanaka, Toyoichi

    PY - 1996

    Y1 - 1996

    N2 - Polyampholytes (PAs) are heteropolymers with long range Coulomb interactions. Unlike polymers with short range forces, PA energy levels have nonvanishing correlations and are thus very different from the random energy model (REM). Nevertheless, if charges in the PA globule are screened as in a regular plasma, PAs freeze in REM fashion. Our results shed light on the potential role of Coulomb interactions in folding and evolution of proteins, which are weakly charged PAs, in particular, making connection with the finding that sequences of charged amino acids in proteins are not random.

    AB - Polyampholytes (PAs) are heteropolymers with long range Coulomb interactions. Unlike polymers with short range forces, PA energy levels have nonvanishing correlations and are thus very different from the random energy model (REM). Nevertheless, if charges in the PA globule are screened as in a regular plasma, PAs freeze in REM fashion. Our results shed light on the potential role of Coulomb interactions in folding and evolution of proteins, which are weakly charged PAs, in particular, making connection with the finding that sequences of charged amino acids in proteins are not random.

    UR - http://www.scopus.com/inward/record.url?scp=0001460708&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0001460708&partnerID=8YFLogxK

    M3 - Article

    VL - 77

    SP - 3565

    EP - 3568

    JO - Physical Review Letters

    JF - Physical Review Letters

    SN - 0031-9007

    IS - 17

    ER -