Entropic Barriers, Frustration and Order: Basic Ingredients in Protein Folding

Details Entropic Barriers, Frustration and Order: Basic Ingredients in Protein Folding Entropic Barriers, Frustration and Order: Basic Ingredients in Protein Folding

1995-12-04

arxiv.org/abs/cond-mat/9512019v1

Physics

Condensed Matter

4 pages, 4 Figures appended as postscript file

Scientific paper

10.1103/PhysRevLett.77.2324

We solve a model that takes into account entropic barriers, frustration, and the organization of a protein-like molecule. For a chain of size $M$, there is an effective folding transition to an ordered structure. Without frustration, this state is reached in a time that scales as $M^{\lambda}$, with $\lambda\simeq 3$. This scaling is limited by the amount of frustration which leads to the dynamical selectivity of proteins: foldable proteins are limited to $\sim 300$ monomers; and they are stable in {\it one} range of temperatures, independent of size and structure. These predictions explain generic properties of {\it in vivo} proteins.

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