title: Mode coupling points to functionally important residues in myosin II.
abstract: Relevance of mode coupling to energy/information transfer during protein function, particularly in the context of allosteric interactions is widely accepted. However, existing evidence in favor of this hypothesis comes essentially from model systems. We here report a novel formal analysis of the near-native dynamics of myosin II, which allows us to explore the impact of the interaction between possibly non-Gaussian vibrational modes on fluctutational dynamics. We show that an information-theoretic measure based on mode coupling alone yields a ranking of residues with a statistically significant bias favoring the functionally critical locations identified by experiments on myosin II.
authors.affiliation: Colleges of Engineering and Sciences, Koç University, Sarıyer, 34450, İstanbul, Turkey; School of Informatics and Computing, Indiana University, Bloomington, Indiana.
authors.forename: Onur
authors.initials: O
authors.lastname: Varol
authors.forename: Deniz
authors.initials: D
authors.lastname: Yuret
authors.forename: Burak
authors.initials: B
authors.lastname: Erman
authors.forename: Alkan
authors.initials: A
authors.lastname: Kabakçıoğlu
mesh_terms: D000495:Allosteric Site; D004023:Dictyostelium / Q000378:metabolism*; D004735:Energy Transfer; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism; D024462:Myosin Type II / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D015800:Protozoan Proteins; D024462:Myosin Type II
keywords: allostery; anharmonicity; mode coupling; molecular dynamics; myosin II