Bulletin of the American Physical Society
2006 APS March Meeting
Monday–Friday, March 13–17, 2006; Baltimore, MD
Session L7: Flexible Molecular Recognition: The New Paradigm |
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Sponsoring Units: DBP Chair: Jin Wang, Stony Brook University Room: Baltimore Convention Center 307 |
Tuesday, March 14, 2006 5:45PM - 6:21PM |
L7.00001: Mis-folding and self-association: opportunities for alternative modes of self-recognition during the folding of TIM barrel proteins Invited Speaker: The ($\beta\alpha$)8 or TIM barrel motif is one of the most common in biology, represented in all three super-kingdoms of life. Detailed thermodynamic and kinetic analysis of the folding reactions of three members of the TIM barrel family of proteins reveal a common propensity to mis-fold to an off-pathway intermediate in less than a few milliseconds. The unfolding of this stopped-flow burst-phase intermediate controls access to an on-pathway intermediate that is highly-populated at moderate denaturant concentrations. Curiously, the equilibrium intermediate for two of the three nominally monomeric proteins spontaneously adopts a dimeric form; the native state of the third also dimerizes at micromolar concentrations. The early mis-folding reactions may reflect the rapid access to non-native folds enabled by the simple, repetitive $\beta\alpha$ topology of this motif. The propensity of stable forms, either intermediate or native, to form dimers may reflect a segment-swapping mechanism enabled by the modular folding of these single structural domain proteins. Off-pathway intermediates and non-native dimers serve as examples of important, alternative intra- or inter-molecular self-recognition events. [Preview Abstract] |
Tuesday, March 14, 2006 6:21PM - 6:57PM |
L7.00002: Dynamics of enzymes. Magnetic resonance methods Invited Speaker: |
Tuesday, March 14, 2006 6:57PM - 7:33PM |
L7.00003: Protein kinases/signal transduction: structure/function Invited Speaker: |
Tuesday, March 14, 2006 7:33PM - 8:09PM |
L7.00004: Flexible protein-protein interactions Invited Speaker: |
Tuesday, March 14, 2006 8:09PM - 8:45PM |
L7.00005: Single Molecule Dynamics Reveals the Role of Flexibility in Bio-molecular Recognition Invited Speaker: With combined single molecule study of flexible protein binding with an energy landscape inspired microscopic model, we found strong evidences of a new paradigm that bio-molecular recognition is determined by flexibilities in addition to structures. The single-molecule study show conformational fluctuations of the protein complex that involves bound and loosely bound states, which can be quantitatively explained in our model as a result of cooperative binding. Theoretical predictions on the key residues are consistent with mutational experiments. The combined study provides a test ground for fundamental mechanisms and insights for future explorations on recognition with large conformational changes. [Preview Abstract] |
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