title: Protein surface and core dynamics show concerted hydration-dependent activation.
abstract: By specifically labeling leucine/valine methyl groups and lysine side chains "inside" and "outside" dynamics of proteins on the nanosecond timescale are compared using neutron scattering. Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.
authors.affiliation: Australian Nuclear Science and Technology Organisation Bragg Institute, Menai NSW, Australia.
authors.forename: Kathleen
authors.initials: K
authors.lastname: Wood
authors.forename: François-Xavier
authors.initials: FX
authors.lastname: Gallat
authors.forename: Renee
authors.initials: R
authors.lastname: Otten
authors.forename: Auke J
authors.initials: AJ
authors.lastname: van Heel
authors.forename: Mathilde
authors.initials: M
authors.lastname: Lethier
authors.forename: Lambert
authors.initials: L
authors.lastname: van Eijck
authors.forename: Martine
authors.initials: M
authors.lastname: Moulin
authors.forename: Michael
authors.initials: M
authors.lastname: Haertlein
authors.forename: Martin
authors.initials: M
authors.lastname: Weik
authors.forename: Frans A A
authors.initials: FA
authors.lastname: Mulder
mesh_terms: D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D014867:Water