Chain Length Scaling of Protein Folding Time

1996/06/24 by A. M. Gutin, Victor Abkevich, V. I. Abkevich +1 · 8 citations
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Protein Structure and Dynamics #Theoretical and Computational Physics #cond-mat #q-bio

paper · pdf · doi:10.1103/physrevlett.77.5433

arxiv created 1996/06/24 · openalex publication_date 1996/12/30 · arxiv updated 2009/11/30 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/28

Abstract

Folding of protein-like heteropolymers into unique 3D structures is investigated using Monte Carlo simulations on a cubic lattice. We found that the folding time of chains of length N scales as N^\ensuremathλ at the temperature of fastest folding. For chains with random sequences of monomers \ensuremathλ\ensuremath≈6, and for chains with sequences designed to provide a pronounced minimum of energy to their ground state conformation \ensuremathλ\ensuremath≈4. Folding at low temperatures exhibits a simple Arrhenius-like behavior.

Citations

• Funnels, pathways, and the energy landscape of protein folding: A synthesis

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