Evidence Of Protein Collective Motions On The Picosecond Time Scale

Details Evidence Of Protein Collective Motions On The Picosecond Time Scale Evidence Of Protein Collective Motions On The Picosecond Time Scale

2010-06-07

arxiv.org/abs/1006.1314v1

Biology

Quantitative Biology

Biomolecules

Scientific paper

We investigate the presence of structural collective motions on a picosecond time scale for the heme protein, cytochrome c, as a function of oxidation and hydration, using terahertz (THz) time-domain spectroscopy and molecular dynamics simulations. The THz response dramatically increases with oxidation, with the largest increase for lowest hydrations and highest frequencies. For both oxidation states the THz response rapidly increases with hydration saturating above ~25% (g H2O/g protein). Quasi-harmonic vibrational modes and dipole-dipole correlation functions are calculated from molecular dynamics trajectories. The collective mode density of states alone reproduces the measured hydration dependence providing strong evidence of the existence of these motions. The large oxidation dependence is reproduced only by the dipole-dipole correlation function, indicating the contrast arises from diffusive motions consistent with structural changes occurring in the vicinity of a buried internal water molecule.

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