Kinetic small angle neutron scattering to study large biomolecular complexes
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Date
2016-11-29
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Volume Title
Publisher
Australian Institute of Nuclear Science and Engineering
Abstract
Proteins are the structural building blocks that make us up but also the functional molecules that drive us. Amazing advances over the last 60 years in structural biology mean we are now determining the 3D structure of over eight thousand proteins per year. Proteins rarely function as isolated entities however, and one of the next major challenges in structural biology is to examine the structure-function relationship in larger complexes made up of several individual proteins.
Small angle scattering is particularly well suited to probe the space scale of large biomolecular complexes. The protein α-Crystallin makes up around a third of the structural proteins of mammalian eye lenses as well as displaying chaperone function. Here we examine the dynamical structure of α-Crystallin complexes by following exchange between the complexes using deuteration and small angle neutron scattering [1].
The work described is a result of collaborative work between all the authors listed below.
Description
Keywords
Proteins, Biology, Molecules, Small angle scattering, Deuteration, Eyes
Citation
Inoue, R., Wood, K. & Sugiyama, M. (2016). Kinetic small angle neutron scattering to study large biomolecular complexes. Paper presented at 13th AINSE-ANBUG Neutron Scattering Symposium, Sydney, NSW, Australia, 29-30 November 2016.