Ontology highlight
ABSTRACT:
SUBMITTER: Ovchinnikov S
PROVIDER: S-EPMC4034769 | biostudies-literature | 2014 May
REPOSITORIES: biostudies-literature
eLife 20140501
Do the amino acid sequence identities of residues that make contact across protein interfaces covary during evolution? If so, such covariance could be used to predict contacts across interfaces and assemble models of biological complexes. We find that residue pairs identified using a pseudo-likelihood-based method to covary across protein-protein interfaces in the 50S ribosomal unit and 28 additional bacterial protein complexes with known structure are almost always in contact in the complex, pr ...[more]