Flavio Seno - Universita di Padova
What determines the structure of native folds in proteins?
The protein folding problem is one of the most important and challenging topics in which complexity can be tackled with the methods and ideas of statistical mechanics. Here we present a simple physical model that demonstrates that the native state folds of proteins can emerge on the basis of considerations of geometry and symmetry. We show that the inherent anisotropy of a chain molecule, the geometrical and energetic constraints placed by the hydrogen bonds and sterics, and hydrophobicity are sufficient to yield a free-energy landscape with broad minima even for a homopolymer. These minima correspond to marginally compact structures comprising the menu of folds that proteins choose from to house their native states in. The results provide a general framework for understanding the common characteristics of globular proteins