Vibrational spectroscopy on aspartate-alpha-decarboxylase enzyme with and without ligand to compare with infrared/Thz spectroscopy
The Aspartate-alpha-decarboxylase (ADC) enzyme is responsible for the assimilation of L-aspartate in bacteria and fungi. D-Serine is an inhibitor of ADC which binds at the active centre and prevents the reaction from completion and causes a conformational change in the C-terminal loop within ADC. This conformational change can be assumed to be associated with a change in the vibrational dynamics as indicated by molecular dynamics simulations carried out by our group. With the proposed experiment we aim to record neutron vibrational spectra on ADC samples with and without the inhibitor to explore the effect of this inhibitor on the vibrational dynamics and compare with infrared and THz spectroscopy as well as with MD simulations. By combining neutron spectroscopy with molecular dynamics simulations and complementary infrared and Thz spectroscopy, we will obtain a conclusive answer to whether a dynamic change exists. Moreover, we will establish the well studied model system ADC as a reference to compare neutron and photon inelastic scattering on biological systems. This proposal is part of the ILL-Hamburg PhD project of T.Raskar.
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Raskar T.; Juliette M. Devos; FORSYTH Victor Trevor; HAERTLEIN Michael; HUSE Nils; JIMENEZ RUIZ Monica; NIEBLING Stephan; PEARSON Arwen and SEYDEL Tilo. (2018). Vibrational spectroscopy on aspartate-alpha-decarboxylase enzyme with and without ligand to compare with infrared/Thz spectroscopy. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-434
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