Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.

Protein folding is in its early stages largely determined by the protein sequence and complex local interactions between amino acids, resulting in lower energy conformations that provide the context for further folding into the native state. We compiled a comprehensive data set of early folding residues based on pulsed labeling hydrogen deuterium exchange experiments. These early folding residues have corresponding higher backbone rigidity as predicted by DynaMine from sequence, an effect also present when accounting for the secondary structures in the folded protein. We then show that the amino acids involved in early folding events are not more conserved than others, but rather, early folding fragments and the secondary structure elements they are part of show a clear trend toward conserving a rigid backbone. We therefore propose that backbone rigidity is a fundamental physical feature conserved by proteins that can provide important insights into their folding mechanisms and stability. Copyright © 2016 Biophysical Society. Published by Elsevier Inc. All rights reserved.

Citation

Rita Pancsa, Daniele Raimondi, Elisa Cilia, Wim F Vranken. Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity. Biophysical journal. 2016 Feb 2;110(3):572-83

PMID: 26840723

search → result