Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.

ABSTRACT:

Background

Folding nucleus of globular proteins formation starts by the mutual interaction of a group of hydrophobic amino acids whose close contacts allow subsequent formation and stability of the 3D structure. These early steps can be predicted by simulation of the folding process through a Monte Carlo (MC) coarse grain model in a discrete space. We previously defined MIRs (Most Interacting Residues), as the set of residues presenting a large number of non-covalent neighbour interactions during such simulation. MIRs are good candidates to define the minimal number of residues giving rise to a given fold instead of another one, although their proportion is rather high, typically [15-20]% of the sequences. Having in mind experiments with two sequences of very high levels of sequenc

SUBMITTER: Banach M 

PROVIDER: S-EPMC4411048 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature