Dynamic structures of globular proteins with respect to correlative movements of residues calculated in the normal mode analysis

摘要: Dynamic structures of globular proteins are studied on the basis correlative movements residues around their native conformations, which computed by means normal mode analysis. To describe dynamic a protein, core regions moving with strong positive or negative correlations to other polypeptide chain detected from correlation maps residues. Such different, according definition, defined geometrical point view, such as secondary structures, domains, modules, and so on. The actually for four proteins, myoglobin, Bence-Jones flavodoxin, hen egg-white lysozyme, different folding types each other. results show that some them coincide but others do not. Then, structure protein is discussed in terms cores detected, compared modules.