Deuteration effects on protein structure and dynamics - comparing high-resolution models of partially deuterated and perdeuterated lysozyme
The function of a protein is intimately linked to its dynamics and the analysis of anisotropic atomic displacement parameters (ADPs) enables information on structural flexibility and local movements to be obtained at atomic level. High-resolution neutron diffraction data can provide unbiased anisotropic ADPs, as routinely derived for small molecules. Similar analyses of proteins has not been done, thus this project can open new opportunities for applications of macromolecular neutron diffraction. This proposal builds on experience from successful experiments at D19, 8-01-475 and 8-01-499 (manuscript in preparation). These high-resolution diffraction data were collected on crystals of partially deuterated HEWL at room temperature and 100 K. This application is for similar measurements on a perdeuterated sample of HEWL. The results will shed light on the crucial question regarding the effect of deuteration on protein structure and dynamics. 14 days are requested at D19, which is the only instrument enabling the (atomic) resolution needed to obtain and refine anisotropic APDs. This proposal is crucial for the PhD program of the main proposer, an ILL funded PhD student.
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RAMOS Joao; FORSYTH Victor Trevor; HAERTLEIN Michael; LANGKILDE Annette Eva; Sine Larsen and MOSSOU Estelle. (2019). Deuteration effects on protein structure and dynamics - comparing high-resolution models of partially deuterated and perdeuterated lysozyme. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-534
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