title: Dissipative dynamics of enzymes.
abstract: We explore enzyme conformational dynamics at sub-Å resolution, specifically, temperature effects. The ensemble-averaged mechanical response of the folded enzyme is viscoelastic in the whole temperature range between the warm and cold denaturation transitions. The dissipation parameter γ of the viscoelastic description decreases by a factor of 2 as the temperature is raised from 10 to 45 °C; the elastic parameter K shows a similar decrease. Thus, when probed dynamically, the enzyme softens for increasing temperature. Equilibrium mechanical experiments with the DNA spring (and a different enzyme) also show, qualitatively, a small softening for increasing temperature.
authors.affiliation: Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.
authors.forename: Amila
authors.initials: A
authors.lastname: Ariyaratne
authors.affiliation: Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.
authors.forename: Chenhao
authors.initials: C
authors.lastname: Wu
authors.affiliation: Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.
authors.forename: Chiao-Yu
authors.initials: CY
authors.lastname: Tseng
authors.affiliation: Department of Physics and Astronomy, University of California, Los Angeles, California 90095, USA.
authors.forename: Giovanni
authors.initials: G
authors.lastname: Zocchi
mesh_terms: D000818:Animals; D004247:DNA / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D049410:Luciferases, Renilla / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D011489:Protein Denaturation; D048790:Renilla / Q000201:enzymology; D012212:Rheology / Q000295:instrumentation / Q000379:methods
chemical_list: D004798:Enzymes; D004247:DNA; D049410:Luciferases, Renilla