title: Large-scale analysis of the dynamics of enzymes.
abstract: Protein enzymes enable the cell to execute chemical reactions in short time by accelerating the rate of the reactions in a selective manner. The motions or dynamics of the enzymes are essential for their function. Comparison of the dynamics of a set of 1247 nonhomologous enzymes was performed. For each enzyme, the slowest modes of motion are calculated using the Gaussian network model (GNM) and they are globally aligned. Alignment is done using the dynamic programming algorithm of Needleman and Wunsch, commonly used for sequence alignment. Only 96 pairs of proteins were identified to have three similar GNM slow modes with 63 of them having a similar structure. The most frequent slowest mode of motion describes a two domains anticorrelated motion that characterizes at least 23% of the enzymes. Therefore, dynamics uniqueness cannot be accounted for by the slowest mode itself but rather by the combination of several slow modes. Different quaternary structure packing can restrain the motion of enzyme subunits differently and may serve as another mechanism that increases the dynamics uniqueness.
authors.affiliation: Department of Computer Sciences and Mathematics, Ariel University, Ariel, 40700, Israel; Department of Molecular Biology, Ariel University, Ariel, 40700, Israel.
authors.forename: Dror
authors.initials: D
authors.lastname: Tobi
mesh_terms: D004798:Enzymes / Q000737:chemistry*; D008962:Models, Theoretical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D004798:Enzymes; D011506:Proteins
keywords: Gaussian network model; dynamics alignment; enzymes; normal mode analysis; protein dynamics