Phase transition in polypeptides: a step towards the understanding of protein folding
Frankfurt Institute for Advanced Studies, Max von Laue Str. 1, 60438 Frankfurt am Main, Germany
Corresponding author: a email@example.com
Revised: 28 August 2006
Published online: 8 November 2006
We present a formalism which turns out to be very successful in the description of the polypeptide folding. We consider this process as a first-order phase transition and develop a theory which is free of model parameters and is based solely on fundamental physical principles. It describes essential thermodynamical properties of the system such as heat capacity, the phase transition temperature and others from the analysis of the polypeptide potential energy surface calculated within ab initio density functional theory and parameterized by two dihedral angles. This problem is viewed as a major breakthrough in the theoretical understanding of the protein folding process. Our conclusion is based on the comparison of the predictions of our theory with the results of several independent experiments.
PACS: 82.60.Fa – Heat capacities and heats of phase transitions / 87.15.He – Dynamics and conformational changes / 64.70.Nd – Structural transitions in nanoscale materials / 64.60.-i – General studies of phase transitions
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag, 2006