Abstract
Spontaneous conformational fluctuations in protein molecules have been recently studied by single molecule detection techniques. In this paper, we report the dynamical conformational fluctuations of Ras, a key protein that regulates various cell signaling dynamics, by using single molecule fluorescence resonance energy transfer. Ras was found to be dynamic, spontaneously taking several multiple meta-stable states and fluctuating between them in the order of msec to sec. The states, however, converged to one specific conformation in the presence of effector molecules. The spontaneous fluctuations allow for the dynamic response to multiple effectors.
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