title: THz absorption spectroscopy of solvated β-lactoglobulin.
abstract: The influence of β-lactoglobulin (βLG) on the fast sub-picosecond collective hydration dynamics in the solvent was investigated by THz absorption spectroscopy as a function of pH. It is well-known that a change in pH from pH 6 to pH 8 reversibly opens or closes the binding cavity by a transition of the E-F loop. Furthermore, the aggregation of the protein into dimers is affected, which is thought to be triggered by changes in the enzyme's electrostatic potential. Our data reveal that pH has a clear influence on the THz absorption of βLG. We discuss this influence in light of the changes observed in the sub-psec solute/solvent dynamics when probed by THz spectroscopy, which are, in turn, seen to correlate with changes in the pH value.
authors.affiliation: Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany.
authors.forename: Hendrik
authors.initials: H
authors.lastname: Vondracek
authors.affiliation: Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany.
authors.forename: Jessica
authors.initials: J
authors.lastname: Dielmann-Gessner
authors.affiliation: Max-Planck-Institut für Chemische Energiekonversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lubitz
authors.affiliation: Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany.
authors.forename: Markus
authors.initials: M
authors.lastname: Knipp
authors.affiliation: Ruhr-Universität Bochum, Universitätsstraße 150, 44780 Bochum, Germany.
authors.forename: Martina
authors.initials: M
authors.lastname: Havenith
mesh_terms: D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry*; D012997:Solvents; D055672:Static Electricity; D055068:Terahertz Spectroscopy; D014867:Water / Q000737:chemistry
chemical_list: D007782:Lactoglobulins; D012997:Solvents; D014867:Water