Combining NMR and SAS for the Study of Protein Structure and Dynamics

Martin Blackledge
Institute de Biologie Structurale, Grenoble, France

Nuclear magnetic resonance (NMR) spectroscopy provides site-specific information about the local conformational behaviour of proteins in solution, and is therefore highly complementary to small angle scattering measurments made on the same samples. In particular residual dipolar couplings, measured in solutions of weakly aligned protein, provide orientational constraints allowing the determination of long-range order in extended or mulitmeric proteins. These constraints can be very powerfully combined with SAS measurements to define supramolecular geometry in solution. In this presentation we will cover the development of such combined approaches for the determination of structure and in particular to probe the dynamic behaviour of folded, partially folded and intrinsically unfolded proteins using SAS and NMR.

Date/time: Friday, 24 October, 9:45