Evidence Of Protein Collective Motions On The Picosecond Time Scale

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

Solvation dynamics of biomolecules: modeling and terahertz experiments

The role of water in biomolecule dynamics has attracted much interest over the past decade, due in part to new probes of biomolecule-water interactions and developments in molecular simulations. Terahertz (THz) spectroscopy, among the most recent experimental methods brought to bear on this problem, is able to detect even small solute induced changes of the collective water network dynamics at the biomolecule-water interface. THz measurements reveal that proteins influence up to 1000 water molecules in their surroundings, and that even small saccharides influence the dynamics of hundreds of surrounding water molecules. The THz spectrum of a protein is sensitive to mutation and depends on the surface charge and flexibility of the protein. Influence on the solvation shell appears most pronounced for native wildtype proteins and decreases upon partial unfolding or mutation. THz spectra of solvated saccharides reveal that the number of water molecules coupled dynamically to a saccharide, forming a dynamical hydration shell around it, is related to the number of exposed oxygen atoms on the solute. The thickness of this layer appears correlated with the bioprotection efficiency of the saccharide. All findings support the thesis of a long-range dynamic coupling between biomolecule and solvent

Terahertz Spectroscopy of Bacteriorhodopsin and Rhodopsin: Similarities and Differences

We studied the low-frequency terahertz spectroscopy of two photoactive protein systems, rhodopsin and bacteriorhodopsin, as a means to characterize collective low-frequency motions in helical transmembrane proteins. From this work, we found that the nature of the vibrational motions activated by terahertz radiation is surprisingly similar between these two structurally similar proteins. Specifically, at the lowest frequencies probed, the cytoplasmic loop regions of the proteins are highly active; and at the higher terahertz frequencies studied, the extracellular loop regions of the protein systems become vibrationally activated. In the case of bacteriorhodopsin, the calculated terahertz spectra are compared with the experimental terahertz signature. This work illustrates the importance of terahertz spectroscopy to identify vibrational degrees of freedom which correlate to known conformational changes in these proteins

Terahertz Time-Domain Spectroscopy of Four Hydroxycinnamic Acid Derivatives

The well-resolved absorption spectra of the hydroxycinnamic acid (HCA) derivatives, caffeic acid, ferulic acid, sinapic acid and chlorogenic acid, were measured over the frequency region from 0.3 to 2.0 THz at 294 K with terahertz time-domain spectroscopy (THz-TDS). Theoretical calculation was applied to assist the analysis and assignment of the individual THz absorption spectra of the HCA derivatives with density functional theory (DFT). The distinctive spectral features were originated from the collective motion of molecules held together by hydrogen bonds. The real and imaginary parts of dielectric function of the four HCA derivatives were also obtained

Optical out-of-plane spin polarization and charge conductivities in spin-orbit-coupled systems in the presence of an in-plane magnetic field

Out-of-plane spin and charge responses to the terahertz field for a clean two-dimensional electron gas with a Rashba spin-orbit interaction in the presence of an in-plane magnetic field are studied. We show that the characteristic optical spectral behavior is remarkably different from that of the system in the absence of in-plane magnetic fields. It is found that the optical spin polarization normal to the plane is nonzero even for this clean system, in sharp contrast to the static case. Due to the combined effect of spin-orbit coupling and in-plane magnetic field, both diagonal and off-diagonal components of optical charge conductivity tensor are nonvanishing. It is indicated that one can control the spin polarization and the optical current by adjusting the optical frequency. In addition, the out-of-plane spin polarization and conductivities strongly rely on the direction of the external magnetic field. Nevertheless, they meet different angle-dependent relations. This dynamical out-of-plane spin polarization could be measured by the time-resolved Kerr rotation technique. Copyright EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg 2010