Print Email Facebook Twitter Evidence of Protein Collective Motions on the Picosecond Timescale Title Evidence of Protein Collective Motions on the Picosecond Timescale Author He, Y. Chen, J.Y. Knab, J.R. Zheng, W. Markelz, A.G. Faculty Applied Sciences Department Imaging Science and Technology Date 2011-02-16 Abstract We investigate the presence of structural collective motions on a picosecond timescale 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). Quasiharmonic vibrational modes and dipole-dipole correlation functions were 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 buried internal water molecules. This source for the observed oxidation dependence is consistent with the lack of an oxidation dependence in nuclear resonant vibrational spectroscopy measurements. To reference this document use: http://resolver.tudelft.nl/uuid:728c4bd8-d1da-4b95-a5a9-9e8e0572b872 DOI https://doi.org/10.1016/j.bpj.2010.12.3731 Publisher Elsevier ISSN 0006-3495 Source Biophysical Journal, 100 (4), 2011 Part of collection Institutional Repository Document type journal article Rights (c) 2011 Biophysical Society Files PDF Knab_2011.pdf 463.67 KB Close viewer /islandora/object/uuid:728c4bd8-d1da-4b95-a5a9-9e8e0572b872/datastream/OBJ/view