Neutron spectroscopy and crystallography combined with THz & fs-infrared spectroscopy: functionally related protein dynamics and structure
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. We will use two exemplar systems; copper amine oxidase (CuAO) and alpha-aspartate decarboxylase (ADC), both from E. coli, where dynamics are proposed to be intimately involved in their catalytic mechanisms.
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Raskar T.; Juliette M. Devos; FORSYTH Victor Trevor; HUSE Nils; KOZA Michael Marek; NIEBLING Stephan; PEARSON Arwen and SEYDEL Tilo. (2018). Neutron spectroscopy and crystallography combined with THz & fs-infrared spectroscopy: functionally related protein dynamics and structure. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-431
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