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    Ben Schuler

    Gilad Haran

    Hagen Hofmann

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    Jane Clarke

    Department of Chemistry, University of Cambridge

    Making Sense of Disorder 

    Monday 04.05.

    7:00 PDT - 10:00 EDT - 14:00 UTC

    15:00 UK - 16:00 CET - 17:00 IL

    Zoom:      Inactive


    Monday 18.05.

    8:00 PDT - 11:00 EDT - 15:00 UTC

    16:00 UK - 17:00 CET - 18:00 IL

    Astbury Centre for Structural and Molecular Biology, University of Leeds

    Early Steps in Amyloid Assembly:

    The Achilles Heel of a Disease Mechanism 

    Many amyloid precursors are intrinsically disordered, while others are folded, yet both can assemble into the highly organised cross-bstructures characteristic of amyloid. Understanding how this conformational transition occurs is not clear, with the initiating steps in aggregation being particularly difficult to study because of the dynamics and heterogeneity of the species involved. Focussing on the IDP α-synuclein (αSyn), linked to pathology in Parkinson’s disease, and b2-microglobulin involved in Dialysis Amyloidosis, I will discuss our understanding of the early steps in amyloid formation and describe how we are beginning to target these steps specifically to prevent amyloid formation. 

    Zoom:       Inactive


    Sheena Radford

    Monday 01.06.

    8:00 PDT - 11:00 EDT - 15:00 UTC

    16:00 UK - 17:00 CET - 18:00 IL

    Ken A. Dill

    Laufer Center for Physical and Quantitative Biology, Stony Brooks University

    How the forces on proteomes manifest as cell behaviors 

    Cells adapt to their environments.  Adaptive forces in homeostasis or evolution are expressed in terms of growth laws and fitness landscapes.  Some aspects of fitness arise from specific actions of individual proteins.  But other aspects arise from more physical, less specific, more universal actions of all proteins in the proteome.  We are modeling how protein folding, aggregation, diffusion, and chaperoning contribute to cellular adaptations.

    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

    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.

    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

    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

    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

    Jane Dyson and Peter Wright

    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.

    Dave Thirumalai

    Department of Chemistry, The University of Texas at Austin

    Iterative Annealing Mechanism for GroEL

    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

    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