Seminars, events & talks

Thursday, 14th April, 2011, 11:00-12:00

Linking function to dynamics in globular, multidomain and unstructured proteins using NMR

A detailed understanding of the biological function of macromolecules requires knowledge of both, their three dimensional structure and their time-dependent fluctuations. Methods to determine the structure of proteins are now well established and the static representations that they provide have contributed much to our understanding of the stability and biological function of proteins (structure-function relationship). In contrast, the characterization of structural fluctuations at atomic resolution is still in its infancy, particularly for motions taking place at biologically relevant time scales (dynamics-function relationship). Such information can be derived from residual dipolar couplings (RDCs) measured by nuclear magnetic resonance (NMR). In this communication we present the determination of native ensembles for globular, multi-domain and disordered proteins that explicitly represent their structural heterogeneity in the sub-millisecond time scale. The detailed descriptions of macromolecular dynamics achieved have allowed us to characterize: i) the transfer of structural information across a surface patch in ubiquitin involved in molecular recognition by the proteins that regulate protein degradation [1], ii) the role of inter-domain motions of T4 Lysozyme in enzymatic catalysis [2], and iii) the native (residual) contacts in chemically denatured ubiquitin that initiate the folding of this protein [3].

Speaker: XAVIER SALVATELLA - Laboratory of Molecular Biophysics, Institute for Research in Biomedicine.

Room Room 473.10 (PRBB - 4th Floor)

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