Biophysical Society 62nd Annual Meeting | Program Guide

Eye Lens Crystallins and the Development of Cataract Disease Workshop 1:00 pm–5:00 pm, South, Level Three, Room 312 The transparency of the eye lens depends on maintenance of the native state of the Greek key γ - and β− crystallins. These proteins define the Greek key fold and have served as models for β -sheet proteins. The α -crystallin chaperones are the original examples of the small heat shock proteins family and the crystallin system has provided important models for subtrate/chaperone action. The γ D-crystallins in the central core of the lens, are synthesized during infancy, and are among the longest-lived proteins in the body. Cataract, the leading cause of blindness worldwide, involves the polymerization of covalently damaged or partially unfolded conformations of the lens crystallins into aggregates large enough to scatter visible light. Congenital cataracts are associated with a number of single amino acid substitutions in γ D-crystallin and other lens crystallins. The folding, unfolding and aggregation of mutant and modified crystallins have been studied in considerable detail, aided by unusual fluorescence properties of the four buried and conserved tryptophan residues in βγ - crystallins. However the results have not accounted for the development of cataracts in the lens environment. Recent experiments have identi- fied more precisely a) the sites on the protein where oxidative damage results in destabilization b) the potential role of copper and zinc binding in driving aggregation, and c) the identification of sterols that can retard aggregation reactions and are candidates for anti-cataract therapy. The transition from a soluble well-folded β -sheet to the polymerized state ap- pears to proceeds through a domain-swapping mechanism. This depends on transient stabilization of a distinctive partially-unfolded β -sheet inter- mediate induced in the mutant or modified protein by temperatures at and above physiological and involves some unexpected thiol chemistry. Co-Chairs Jonathan King, MIT Liliana Quintanar, CINVESTAV, Mexico Presenters

Symposium in Memory of Kamal Shukla 1:20 pm–5:40 pm, Esplanade, Room 154 For 25 years, Kamal Shukla helped shape molecular biophysics in the United States and abroad. In his role as the leader of the Molecular Biophysics Cluster in the Biological Science Directorate at the National Science Foundation, Dr. Shukla seeded and promoted the careers of an entire generation of biophysicists. His vision for the development of quantitative, theoretical and physical approaches to the study of biologi- cal systems, and his success and accomplishments, live on in the thriving community he left behind. For his contributions to biophysics he received the prestigious Distinguished Service Award from the Biophysical Society in 2015. 12:45 pm REGISTRATION 1:20 pm WELCOME AND OPENING REMARKS Bertrand Garcia-Moreno SESSION I Chair, Susan Marqusee, University of California, Berkeley 1:30 pm José Onuchic, Rice University 1:45 pm Catherine A. Royer, Rensselaer Polytechnic Institute 2:10 pm Gaetano Montelione, Rutgers University 2:35 pm C. Robert Matthews, University of Massachusetts 3:00 pm COFFEE BREAK SESSION II Chair, Catherine A. Royer, Rensselaer Polytechnic Institute 3:30 pm Joan Emma Shea, University of California, Santa Barbara 3:55 pm Neal Woodbury, Arizona State University 4:20 pm Dave Thirumalai, University of Texas at Austin 4:45 pm WilliamMoerner, Stanford University 5:10 pm Wilson Francisco, NSF 5:25 pm Krastan Blagoev, NSF 5:40 pm CLOSING REMARKS Registration 3:00 pm–5:00 pm, South Lobby New Council Orientation 3:30 pm–4:30 pm, Marriott Marquis, Sierra H Joint Council Reception, Dinner, and Meeting 5:00 pm–9:00 pm, Marriott Marquis, Foothill C

F R I D A Y

Jose Antonio Dominguez Calva, CINVESTAV, Mexico Jason Gestwicki, University of California, San Francisco Jonathan King, MIT Kirsten Lampi, Oregon Health Science Center Rachel Martin, University of California, Irvine

Liliana Quintanar, CINVESTAV, Mexico Eugene Serebryany, Harvard University Thanks to the MIT International Science and Technology Initiative for US/ Mexico Collaboration, for support of this workshop.

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