Distinguished Scientist Lecture Series Presents
Protein Folding: Seeing is Deceiving
Thursday, March 30, 2017
Reem-Kayden Center Laszlo Z. Bito '60 Auditorium
7:00 pm EDT/GMT-4
7:00 pm EDT/GMT-4
Once you eliminate the impossible, whatever remains, no matter how improbable,
must be the truth. -Sherlock Holmes
George Rose
Jenkins Dept. of Biophysics
Johns Hopkins University
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.must be the truth. -Sherlock Holmes
George Rose
Jenkins Dept. of Biophysics
Johns Hopkins University
For more information, call 845-752-2309, or e-mail [email protected].
Time: 7:00 pm EDT/GMT-4
Location: Reem-Kayden Center Laszlo Z. Bito '60 Auditorium