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Hello, The following event may be of interest to you: Protein Folding: Seeing is Deceiving Thursday, March 30, 2017 We challenge the time-honored conviction that proteins realize their native folds via specific favorable interactions, proposing instead that an imprint of the fold is selected primarily by elimination of unfavorable interactions. Two types of energetically disfavored interactions are considered here: steric clashes and polar groups lacking hydrogen-bond partners. Both types are largely excluded from the thermodynamic population, winnowing that population progressively as the protein becomes compact. Compaction is accompanied by the entropically favored release of solvent shells around apolar groups. Remarkably, both solvent shell release and excluding interactions are somewhat non-specific, yet together they promote highly specific chain organization. For example, exhaustive conformational enumeration of a test hexapeptide reduces 1.5x1012 conceivable conformations to the experimentally-determined dominant population in aqueous solution – this despite deliberate neglect of attractive interactions. Time: 7:00 pm EDT/GMT-4 Location: Reem-Kayden Center Laszlo Z. Bito '60 Auditorium Sponsor: Distinguished Scientist Lecture Series Contact: Michael Tibbetts. E-mail: [email protected] Phone: 845-752-2309 If you would like to see more events please visit the following URL: http://www.bard.edu/academics/programs/physics/events/