title: Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements.
abstract: We have investigated microsecond to millisecond time scale dynamics in several key hydrophobic core methyl groups of chicken villin headpiece subdomain protein (HP36) using a combination of single-site labeling, deuteron solid-state NMR line shape analysis, and computational modeling. Deuteron line shapes of hydrated powder samples are dominated by rotameric jumps and show a large variability of rate constants, activation energies, and rotameric populations. Site-specific activation energies vary from 6 to 38 kJ/mol. An additional mode of diffusion on a restricted arc is significant for some sites. In dry samples, the dynamics is quenched. Parameters of the motional models allow for calculations of configurational entropy and heat capacity, which, together with the rate constants, allow for observation of interplay between thermodynamic and kinetic picture of the landscape. Mutations at key phenylalanine residues at both distal (F47L&F51L) and proximal (F58L) locations to a relatively rigid side chain of L69 have a pronounced effect on alleviating the rigidity of this side chain at room temperature and demonstrate the sensitivity of the hydrophobic core environment to such perturbations.
authors.affiliation: Department of Chemistry, University of Alaska, Anchorage, Alaska 99508, United States. aflv@uaa.alaska.edu
authors.forename: Liliya
authors.initials: L
authors.lastname: Vugmeyster
authors.forename: Dmitry
authors.initials: D
authors.lastname: Ostrovsky
authors.forename: Anastasia
authors.initials: A
authors.lastname: Khadjinova
authors.forename: Jeremy
authors.initials: J
authors.lastname: Ellden
authors.forename: Gina L
authors.initials: GL
authors.lastname: Hoatson
authors.forename: Robert L
authors.initials: RL
authors.lastname: Vold
mesh_terms: D000818:Animals; D002645:Chickens; D003903:Deuterium; D019277:Entropy; D057927:Hydrophobic and Hydrophilic Interactions; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010649:Phenylalanine; D012997:Solvents / Q000737:chemistry
chemical_list: D008840:Microfilament Proteins; D012997:Solvents; C026615:villin; D010649:Phenylalanine; D003903:Deuterium
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