title: Separability between overall and internal motion: a protein folding problem.
abstract: The separability between overall and internal motions is evaluated over multiple folding trajectories of the villin headpiece subdomain. The analysis, which relies on the Prompers-Brüschweiler separability index, offers a potentially useful perspective on protein folding. The protein is considered folded in this study, not when it reaches some static target, but rather when it tumbles as a dynamically constrained object. The analysis also demonstrates how the separability index, when applied to protein folding simulations, can facilitate the analysis of NMR relaxation data.
authors.affiliation: Department of Chemistry and Physical Sciences, College of Mount St. Joseph, Cincinnati, OH 45233, USA. eric_johnson@mail.msj.edu
authors.forename: Eric
authors.initials: E
authors.lastname: Johnson
mesh_terms: D008840:Microfilament Proteins / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D008840:Microfilament Proteins; D011506:Proteins; C026615:villin