Heteropolymer freezing and design: Towards physical models of protein folding

Journal Article · Sat Jan 01 04:00:00 EST 2000 · Reviews of Modern Physics

DOI:https://doi.org/10.1103/RevModPhys.72.259· OSTI ID:20215567

Pande, Vijay S ^[1]; Grosberg, Alexander Yu ^[2]; Tanaka, Toyoichi ^[3]

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1. Chemistry Department, Stanford University, Stanford, California 94305-5080 (United States)
2. Department of Physics, University of Minnesota, Minneapolis, Minnesota 55455 (United States)
3. Department of Physics and Center for Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 (United States)

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 T{sup des} 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. (c) 2000 The American Physical Society.

• OSTI ID: 20215567
• Journal Information: Reviews of Modern Physics, Journal Name: Reviews of Modern Physics Journal Issue: 1 Vol. 72; ISSN 0034-6861; ISSN RMPHAT
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
60 APPLIED LIFE SCIENCES
CONFORMATIONAL CHANGES
EXPERIMENTAL DATA
FREEZING
MOLECULAR BIOLOGY
MOLECULAR MODELS
PHASE TRANSFORMATIONS
POLYMERS
PROTEINS
REVIEWS
THEORETICAL DATA