Protein deuteration extending structural characterisations by small angle neutron scattering with contrast variation.
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Date
2020-11-11
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Volume Title
Publisher
Australian Institute of Nuclear Science and Engineering (AINSE)
Abstract
Protein deuteration enables unique applications of neutron scattering o the life sciences, at both low and high resolutions. In recent years, the National Deuteration Facility at ANSTO have developed and published a robust and efficient method of recombinant protein deuteration.[1] Utilising this method enables us to routinely collaborate with life scientists by removing the difficulty of biomolecule deuteration from their needs for sample preparation to make best use of neutron scattering. In this presentation I will highlight the essential role of protein deuteration in the structural characterization of previously poorly characterized “suppressor of copper sensitivity” proteins, as recently published.[2] Using this, and more recent work in progress, I will illustrate the value of small angle scattering as a complementary method to high resolution techniques so as to including disordered to-ordered transitions that are frequently the basis for functional mechanisms in life and disease. Other applications of protein deuteration, for neutron reflectometry, neutron crystallography, and nuclear magnetic resonance, will be briefly explained.
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Keywords
Scattering, ANSTO, Australia, Proteins, Small angle scattering, Copper
Citation
Duff, A. (2020). Protein deuteration extending structural characterisations by small angle neutron scattering with contrast variation. Paper presented to the ANBUG-AINSE Neutron Scattering Symposium, AANSS 2020, Virtual Meeting, 11th - 13th November 2020. (pp. 16). Retrieved from: https://events01.synchrotron.org.au/event/125/contributions/3741/contribution.pdf