DOI: 0906.0297Jun 17, 2009Paper

Nanosecond motions in proteins impose bounds on the timescale distributions of local dynamics

ArXiv
Osman Burak OkanCanan Atilgan

Abstract

We elucidate the physics of the dynamical transition via 10-100ns molecular dynamics simulations at temperatures spanning 160-300K. By tracking the energy fluctuations, we show that the protein dynamical transition is marked by a cross-over from piecewise stationary to stationary processes that underlie the dynamics of protein motions. A two-time-scale function captures the non-exponential character of backbone structural relaxations. One is attributed to the collective segmental motions and the other to local relaxations. The former is well-defined by a single-exponential, nanosecond decay, operative at all temperatures. The latter is described by a set of processes that display a distribution of time-scales. Though their average remains on the picosecond time-scale, the distribution is markedly contracted at the onset of the transition. The collective motions are shown to impose bounds on time-scales spanned by local dynamical processes. The piecewise stationary character below the transition implicates the presence of a collection of sub-states whose interactions are restricted. At these temperatures, a wide distribution of local motion time-scales, extending beyond that of nanoseconds is observed. At physiological tempera...Continue Reading

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