Neutron spectroscopy & crystallography combined with THz spectroscopy: complementary methods for the study of protein dynamics
Structural biology aims to relate structure to function, but obtaining detailed information about functional dynamics remains challenging. Although crystallographic structures encode information about dynamics, this cannot be routinely extracted. In contrast, spectroscopy provides detailed dynamic information, but not an overall structural picture of the conformational variation associated with it. Further, integrating the information obtained from disparate biophysical methods is difficult as they probe dynamics and structure on different length- and time-scales, as well as different states (solutions, powders and crystals). We will address this by taking an interdisciplinary approach, combining neutron spectroscopy and crystallography with THz vibrational spectroscopy. Crucially our experiments will be carried out on the same proteins, prepared in the same way, in order to enable us to truly compare the data obtained from each experimental method. In this proposal we will study the E. coli enzyme copper amine oxidase (CuAO), where dynamics are proposed to be intimately involved in its catalytic mechanisms.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
PEARSON Arwen; Matthew P. Blakeley; COQUELLE Nicolas; FORSYTH Victor Trevor; HUSE Nils; NIEBLING Stephan; Raskar T. and SEYDEL Tilo. (2017). Neutron spectroscopy & crystallography combined with THz spectroscopy: complementary methods for the study of protein dynamics. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-428
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This data is not yet public
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