title: Experiments with proteins at low temperature: what do we learn on properties in their functional state?
abstract: The authors compared the spectral response of Zn-substituted horseradish peroxidase in a glycerol/water solvent to hydrostatic pressure at 2 K and ambient temperature. The low temperature experiments clearly demonstrate the presence of at least three different conformations with drastically different elastic properties. However, the main conformation, which determines the fluorescence spectrum at ambient temperature, did not show any significant difference between low and high temperature and pressure. The authors conclude that the local compressibility of the heme pocket of the protein depends only very weakly on temperature.
authors.affiliation: Physik-Department E14, Technische Universität München, 85354 Freising, Germany.
authors.forename: V V
authors.initials: VV
authors.lastname: Ponkratov
authors.forename: J
authors.initials: J
authors.lastname: Wiedersich
authors.forename: J
authors.initials: J
authors.lastname: Friedrich
authors.forename: J M
authors.initials: JM
authors.lastname: Vanderkooi
mesh_terms: D006418:Heme / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006874:Hydrostatic Pressure; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013696:Temperature; D015032:Zinc / Q000737:chemistry*
chemical_list: D006418:Heme; D006735:Horseradish Peroxidase; D015032:Zinc