Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.
Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.
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DOI:
10.1016/j.str.2011.01.011
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发表时间:
2011-04-13
期刊:
影响因子:
5.7
通讯作者:
Bowen, Mark E.
中科院分区:
文献类型:
--
作者:
Choi, Ucheor B.;McCann, James J.;Weninger, Keith R.;Bowen, Mark E.
Intrinsically disordered proteins (IDPs) participate in critical cellular functions that exploit the flexibility and rapid conformational fluctuations of their native state. Limited information about the native state of IDPs can be gained by the averaging over many heterogeneous molecules that is unavoidable in ensemble approaches. We used single molecule fluorescence to characterize native state conformational dynamics in five synaptic proteins confirmed to be disordered by other techniques. For three of the proteins, SNAP-25, synaptobrevin and complexin, their conformational dynamics could be described with a simple semi-flexible polymer model. Surprisingly, two proteins, neuroligin and the NMDAR-2B glutamate receptor, were observed to stochastically switch among distinct conformational states despite the fact that they appeared intrinsically disordered by other measures. The hop-like intramolecular diffusion found in these proteins is suggested to define a class of functionality previously unrecognized for IDPs.
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