Heteropolymer freezing and design: Towards physical models of protein folding

Vijay S. Pande, Alexander Yu Grosberg, Toyoichi Tanaka

    Research output: Contribution to journalArticle


    Protein folding has become one of the most actively studied problems in modern molecular biophysics. Approaches to the problem combine ideas from the physics of disordered systems, polymer physics, and molecular biology. Much can be learned from the statistical properties of model heteropolymers, the chain molecules having different monomers in irregular sequences. Even in highly evolved proteins, there is a strong random element in the sequences, which gives rise to a statistical ensemble of sequences for a given folded shape. Simple analytic models give rise to phase transitions between random, glassy, and folded states, depending on the temperature T and the design temperature Tdes of the ensemble of sequences. Besides considering the analytic results obtainable in a random-energy model and in the Flory mean-field model of polymers, the article reports on confirming numerical simulations.

    Original languageEnglish (US)
    Pages (from-to)259-314
    Number of pages56
    JournalReviews of Modern Physics
    Issue number1
    StatePublished - Jan 1 2000


    ASJC Scopus subject areas

    • Physics and Astronomy(all)

    Cite this

    Pande, V. S., Grosberg, A. Y., & Tanaka, T. (2000). Heteropolymer freezing and design: Towards physical models of protein folding. Reviews of Modern Physics, 72(1), 259-314.