Diversity in Free Energy Landscape of Proteins with the Same Native Topology

Details Diversity in Free Energy Landscape of Proteins with the Same Native Topology Diversity in Free Energy Landscape of Proteins with the Same Native Topology

2005-12-09

arxiv.org/abs/q-bio/0512020v2

Chem. Phys. Lett. 427 (2006) 414-417

Biology

Quantitative Biology

Biomolecules

4 pages, 3 figures

Scientific paper

10.1016/j.cplett.2006.05.112

In order to elucidate the role of the native state topology and the stability of subdomains in protein folding, we investigate free energy landscape of human lysozyme, which is composed of two subdomains, by Monte Carlo simulations. A realistic lattice model with Go-like interaction is used. We take the relative interaction strength (stability, in other word) of two subdomains as a variable parameter and study the folding process. A variety of folding process is observed and we obtained a phase diagram of folding in terms of temperature and the relative stability. Experimentally-observed diversity in folding process of c-type lysozimes is thus understood as a consequence of the difference in the relative stability of subdomains.

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