title: Principal components of the protein dynamical transition.
abstract: Proteins exhibit a solvent-driven dynamical transition at 180-220 K, manifested by nonlinearity in the temperature dependence of the average mean-square displacement. Here, molecular dynamics simulations of hydrated myoglobin show that the onset of the transition at approximately 180 K is characterized by the appearance of a single double-well principal component mode involving a global motion of two groups of helices. As the temperature is raised a few more quasiharmonic and multiminimum components successively appear. The results indicate an underlying simplicity in the protein dynamical transition.
authors.affiliation: Computational Molecular Biophysics, Interdisciplinary Center for Scientific Computing (IWR), Im Neuenheimer Feld 368, Universität Heidelberg, 69120 Heidelberg, Germany.
authors.forename: Alexander L
authors.initials: AL
authors.lastname: Tournier
authors.forename: Jeremy C
authors.initials: JC
authors.lastname: Smith
mesh_terms: D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D025341:Principal Component Analysis; D011487:Protein Conformation; D014867:Water / Q000737:chemistry
chemical_list: D009211:Myoglobin; D014867:Water