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ABSTRACT:
SUBMITTER: Kurzbach D
PROVIDER: S-EPMC5338234 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Kurzbach Dennis D Flamm Andrea G AG Sára Tomáš T
Protein science : a publication of the Protein Society 20160616 9
A graph theoretical analysis of nuclear magnetic resonance (NMR) data of six different protein interactions has been presented. The representation of the protein interaction data as a graph or network reveals that all of the studied interactions are based on a common functional concept. They all involve a single densely packed hub of functionally correlated residues that mediate the ligand binding events. This is found independent of the kind of protein (folded or unfolded) or ligand (protein, p ...[more]