Essential dynamics of cold denaturation proteins: Model frataxin Yfh1

YANIS RICARDO ESPINOSA SILVA, RAUL GRIGERA; ERNESTO CAFFARENA

Bahía Blanca

Congreso; VI Argentinian Conference on Bioinformatics and Computational Biology; 2015

The transition from folding to unfolding on decreasing the temperature, is a property of globular proteins that have been considered in the literature, however the explanation of the process is still on debate. A sensible explanation is the approach from Gibbs-Helmholtz equation considering the diminishing of hydrophobic interaction, and then, allowing the hydration of non-polar groups at low temperature . Due to the drastically changes of the protein structure to avoid freezing, any possible experimental data obtained may not describe appropriated a possible extrapolation to the protein native state. We have chosen as alternative approach the simulation using molecular dynamics, analyzing the protein motions by essential dynamics.