Research Problem) The nature of protein-protein interactions
How do proteins interact? When one protein binds to another, one or both changes conformation. Two hypothesis have been proposed to describe such binding: in the induced fit model, the interaction between a protein and a ligand induces a conformation change (in the protein or ligand) through a stepwise process. In the conformational selection model, the unliganded protein (in the absence of the ligand) exists as an ensemble of conformations in a dynamic equilibrium. The binding ligand interacts preferentially with one among many of these conformations and shifts the equilibrium in favor of the selected conformation. Three recent papers shed light on this question: Boehr, D. and Wright, R.E., 2008. How do proteins interact?Science 320:1429-1430. Gsponer. J. et al. 2008. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure 16:736-746.
Lange, O.F., et al., Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.Science 320:1471-1475.
What proteins were studied in these papers?
What techniques were used, and what time scales of protein motion were studied?
What were the conclusions of these papers, and how do these results illuminate the choice between induced fit and conformational selection in protein-protein interactions.?
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