title: Compressibility gives new insight into protein dynamics and enzyme function.
abstract: The adiabatic compressibility of enzyme is largely influenced by binding of coenzyme and substrate, due to the changes in atomic packing. Amino acid substitution also induces large changes in compressibility parallel to enzyme activity. These results demonstrate that a small alteration of local structure by ligand binding and mutation is dramatically magnified in the flexibility of protein molecule to affect the function. Compressibility gives new insight into protein dynamics and enzyme function from the aspect of atomic packing or cavity which cannot be obtained by other techniques.
authors: Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Japan. gekko@sci-hiroshima-u.ac.jp
authors: Kunihiko
authors: K
authors: Gekko
mesh_terms: D019943:Amino Acid Substitution; D004798:Enzymes / Q000737:chemistry / Q000502:physiology*; D008024:Ligands; D011312:Pressure; D011506:Proteins / Q000737:chemistry* / Q000502:physiology
chemical_list: D004798:Enzymes; D008024:Ligands; D011506:Proteins