Proteins and protein complexes carry out much of the practical biological work of the cell: RNA polymerases transcribe DNA to RNA, ribosomes translate RNA to polypeptide chains, chaperones assist the folding of polypeptide chains into functional proteins, the nuclear pore complex transports selectively molecular cargo between the cytoplasm and nucleus, and molecular motors transport cargo along cytoskeletal filament tracks to enable cell growth and division. While the static structure of proteins provides invaluable insight into their mechanism of action, their conformational dynamics provide additional important information that often cannot be inferred from static structure alone. Which regions of the molecule are flexible, and which regions are correlated with one another during large-scale, collective motions? In conformational transitions between active and inactive conformers, which regions of the molecule undergo conformational strain and which regions are rigid? Answers to these questions are provided in part by the conformational dynamics of proteins and protein assemblies presented in the Conformational Dynamics Data Bank.

Kim DN, Altschuler J, Strong C, McGill G, Bathe M (2011) Conformational dynamics data bank: a database for conformational dynamics of proteins and supramolecular protein assemblies. Nucleic Acids Research 39(Database issue): D451-5. [ PubMed ]