Ontology highlight
ABSTRACT:
SUBMITTER: Perunov N
PROVIDER: S-EPMC3970890 | biostudies-literature | 2014 Apr
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20140219 4
Various studies suggest that the hydrophobic effect plays a major role in driving the folding of proteins. In the past, however, it has been challenging to translate this understanding into a predictive, quantitative theory of how the full pattern of sequence hydrophobicity in a protein shapes functionally important features of its tertiary structure. Here, we extend and apply such a phenomenological theory of the sequence-structure relationship in globular protein domains, which had previously ...[more]