Low energy pathways for reproducible in vivo protein folding
Abstract
Two proteins, one belonging to the mainly alpha class and the other belonging to the alpha/beta class, are selected to test a kinetic mechanism for protein folding. Targeted molecular dynamics is applied to generate folding pathways for those two proteins, starting from two well defined initial conformations: a fully extended and a alpha-helical conformation. The results show that for both proteins the alpha-helical initial conformation provides overall lower energy pathways to the native state. For the alpha/beta protein, 30 % (40%) of the pathways from an initial alpha-helix (fully extended) structure lead to unentangled native folds, a success rate that can be increased to 85 % by the introduction of a well-defined intermediate structure. These results open up a new direction in which to look for a solution to the protein folding problem, as detailed at the end.
Keywords
Cite
@article{arxiv.1101.0566,
title = {Low energy pathways for reproducible in vivo protein folding},
author = {Leonor Cruzeiro},
journal= {arXiv preprint arXiv:1101.0566},
year = {2011}
}
Comments
Submitted to PRL on the 21st September 2010, rejected by PRL on the 20th December 2010