Ontology highlight
ABSTRACT:
SUBMITTER: Pancsa R
PROVIDER: S-EPMC4744172 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Pancsa Rita R Raimondi Daniele D Cilia Elisa E Vranken Wim F WF
Biophysical journal 20160201 3
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 p ...[more]