Probing protein multidimensional conformational fluctuations by single-molecule multiparameter photon stamping spectroscopy.

ABSTRACT: Conformational motions of proteins are highly dynamic and intrinsically complex. To capture the temporal and spatial complexity of conformational motions and further to understand their roles in protein functions, an attempt is made to probe multidimensional conformational dynamics of proteins besides the typical one-dimensional FRET coordinate or the projected conformational motions on the one-dimensional FRET coordinate. T4 lysozyme hinge-bending motions between two domains along α-helix have been probed by single-molecule FRET. Nevertheless, the domain motions of T4 lysozyme are rather complex involving multiple coupled nuclear coordinates and most likely contain motions besides hinge-bending. It is highly likely that the multiple dimensional protein conformational motions beyond the ty

SUBMITTER: Lu M 

PROVIDER: S-EPMC4199541 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature