Free Energy Self-Averaging in Protein-Sized Random Heteropolymers

Details Free Energy Self-Averaging in Protein-Sized Random Heteropolymers Free Energy Self-Averaging in Protein-Sized Random Heteropolymers

2001-02-05

arxiv.org/abs/cond-mat/0102065v1

Published in Phys. Rev. Lett. Vol. 87, article no. 010102 (2001).

Physics

Condensed Matter

Soft Condensed Matter

4 pages, 3 figures

Scientific paper

10.1103/PhysRevLett.87.078104

Current theories of heteropolymers are inherently macrpscopic, but are applied to folding proteins which are only mesoscopic. In these theories, one computes the averaged free energy over sequences, always assuming that it is self-averaging -- a property well-established only if a system with quenched disorder is macroscopic. By enumerating the states and energies of compact 18, 27, and 36mers on a simplified lattice model with an ensemble of random sequences, we test the validity of the self-averaging approximation. We find that fluctuations in the free energy between sequences are weak, and that self-averaging is a valid approximation at the length scale of real proteins. These results validate certain sequence design methods which can exponentially speed up computational design and greatly simplify experimental realizations.

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