title: Inelastic X-ray scattering studies of the short-time collective vibrational motions in hydrated lysozyme powders and their possible relation to enzymatic function.
abstract: High-resolution inelastic X-ray scattering was used to investigate the collective vibrational excitations in hydrated lysozyme powders as a function of hydration level and temperature. It is found that the samples with strong enzymatic function are "soft", in the sense that they exhibit low frequency and large amplitude intraprotein collective vibrational motions on certain length scales. This is not the case for samples with weak or no enzymatic activity. Thus, we identify a possible correlation between the short-time intraprotein collective vibrational motions and the establishment of enzymatic function in hydrated lysozyme powders, and bring new insight to notions of protein "conformational flexibility" and "softness" in terms of these motions.
authors.affiliation: Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
authors.forename: Zhe
authors.initials: Z
authors.lastname: Wang
authors.forename: Christopher E
authors.initials: CE
authors.lastname: Bertrand
authors.forename: Wei-Shan
authors.initials: WS
authors.lastname: Chiang
authors.forename: Emiliano
authors.initials: E
authors.lastname: Fratini
authors.forename: Piero
authors.initials: P
authors.lastname: Baglioni
authors.forename: Ahmet
authors.initials: A
authors.lastname: Alatas
authors.forename: E Ercan
authors.initials: EE
authors.lastname: Alp
authors.forename: Sow-Hsin
authors.initials: SH
authors.lastname: Chen
mesh_terms: D008958:Models, Molecular; D009038:Motion; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D012542:Scattering, Radiation; D013696:Temperature; D013997:Time Factors; D014732:Vibration; D014867:Water / Q000737:chemistry; D014965:X-Rays
chemical_list: D014867:Water; D009113:Muramidase