Disordered proteins, aggregation and disease

University of California, Berkeley; Lawrence Berkeley National Laboratory

Flexibility in proteins was recognized as a necessary property for function, but large scale disorder in proteins was defined only by NMR studies ≈ 20 years ago. The roles of disordered domains are diverse, and their their characterization challenging. Here I will describe a disordered domain from a bacterial polymerase subunit, sigma54, and how it changes upon interaction with other components of the transcription machinery. I will also briefly discuss and effort to combine NMR and MD simulations to better define disordered protein conformational ensembles.


David Wemmer did his B.S. at UCDavis (1973), Ph.D. at UCBerkeley (1978) with Pines, doing solid state and multiple quantum NMR. After a short postdoc in Dortmund, he moved Stanford and learned about NMR in biological systems, a period when 2D methods were just being applied to protein structure determination. In 1982 he moved to UW in Seattle, where work focused on DNA structure by NMR. In 1985 he returned to Berkeley on the faculty, and continued to study diverse biological systems including drug-DNA complexes, regulatory proteins, and molecular imaging with hyperpolarized xenon.

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