Two state behavior in a solvable model of β-hairpin folding

Chinlin Guo, Herbert Levine, David A. Kessler

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Understanding the mechanism of protein secondary structure formation is an essential part of the protein-folding puzzle. Here we describe a simple model for the formation of a ² hairpin, motivated by the fact that folding of a ² hairpin captures much of the basic physics of protein folding. The modeled hairpin is composed of two interacting Gaussian chains with one pairwise (two-body) and two many-body interactions. We show that these many-body interactions, arising from side chain packing effects, are responsible for producing an “all-or-none” folding transition. We also estimate the (single exponential) folding/unfolding rate via calculating the thermodynamic weight of the “critical” droplet/bubble.

Original languageEnglish
Pages (from-to)3490-3493
Number of pages4
JournalPhysical Review Letters
Issue number15
StatePublished - 10 Apr 2000


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