Monday 15.06.

8:00 PDT - 11:00 EDT - 15:00 UTC

16:00 UK - 17:00 CET - 18:00 IL

Lewis E. Kay

Department of Molecular Genetics, Biochemistry and Chemistry, University of Toronto

The important role of dynamics in the function and misfunction of molecular machines

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Protein molecules play critical roles in cellular function and they catalyze many of the biochemical reactions that are necessary for life. The three-dimensional shapes of these molecules are crucial for guiding proper function and they can change with time due to interactions with other molecules, various stresses on the cell or simply the result of random fluctuations. Although very detailed static pictures of protein molecules have been produced using traditional biophysical tools, macromolecular function and misfunction is, in many cases, intimately coupled to flexibility and knowledge of molecular motions therefore becomes critical. For the past 3 decades my laboratory has developed biophysical techniques, focusing on solution based Nuclear Magnetic Resonance spectroscopy for the study of biomolecular dynamics. A brief description of some of the methods we have derived will be given along with examples to illustrate the critical importance of dynamics to protein function and misfunction.

Zoom:       Inactive

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Martin Gruebele

Department of Chemistry, University of Illinois at Urbana-Champaign

Protein folding and association dynamics: from in silico to in vitro to in vivo

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Protein folding and binding reactions are generally quite fast and involve small free energy differences. As a result, they can be sensitive to the environment that biases protein energy landscapes. I will discuss molecular dynamics simulations, test-tube experiments, in-cell measurements, and measurements in living animals that highlight the sensitivity of protein dynamics to its solvation environment.

Monday 29.06.

8:00 PDT -  11:00 EDT - 15:00 UTC

16:00 UK - 17:00 CET - 18:00 IL

Zoom:       Inactive

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Monday 13.07.

8:00 PDT -  11:00 EDT - 15:00 UTC

16:00 UK - 17:00 CET - 18:00 IL

Jane Dyson

Department of Integrative Structural and Computational Biology, The Scripps Research Institute

NMR Dynamics Studies of Protein Folding Intermediates

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Jane Dyson and Peter Wright

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The transient intermediate states that are populated as a protein folds are difficult to access and study. Both kinetic and equilibrium biophysical methods have been used to probe these states, using chemically or physically unfolded and partly folded states as models. NMR gives unique information on the local motions of a protein chain. The ps-ns time scale motions of the polypeptide backbone in unfolded and partly folded states, measured using relaxation rates, can give important insights into the factors that contribute to progress along the folding pathway. In addition, we can study states at low populations within a conformational ensemble using relaxation dispersion measurements that probe ms-ms motions, which are of particular interest in the folding processes of proteins.

Zoom:      https://weizmann.zoom.us/j/96005573587?pwd=Q25SdGE2NXRuVW5ocWNqQkgvMVdZdz09   

YouTube: TBA

Dave Thirumalai

Department of Chemistry, The University of Texas at Austin

Iterative Annealing Mechanism for GroEL

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Most cytosolic proteins fold spontaneously as envisioned by Anfinsen. However, there are number of proteins that require the chaperone machinery to reach their functionally competent states. Using theory, simple arguments, and simulations using coarse-grained models I will describe the workings of the E. Coli. chaperonin GroEL.  A framework based on the Iterative Annealing Mechanism that unifies inefficient folding under non-permissive conditions, GroEL allostery, and function will be presented.  If time permits some open problems will be discussed.

Monday 27.07.

8:00 PDT -  11:00 EDT - 15:00 UTC

16:00 UK - 17:00 CET - 18:00 IL

Zoom:       TBA

YouTube: TBA

Peter G. Wolynes

Department of Chemistry, Rice University

Protein Dynamics and the Brain

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The brain is a molecular computer. How the brain computes, and feels and learns and remembers remain great mysteries. Neurobiologists have, however, identified some key protein actors in the mechanisms of learning and memory. I will describe some theoretical and computational efforts in understanding some of the molecular aspects of 1) Hebbian learning through the regulatable assembly of the actin cytoskeleton in dendritic spines, 2) the hypothesis that long-term memory involves a functional prion protein and 3) some aspects of the physical chemistry of aggregation processes that are involved in the pathogenesis of Huntington’s disease and Alzheimer’s disease. 

Monday 10.08.

8:00 PDT -  11:00 EDT - 15:00 UTC

16:00 UK - 17:00 CET - 18:00 IL

Zoom:       TBA

YouTube: TBA