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Register a new userThree-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin
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Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.
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Three dimensional (3D) Dirac semimetals which can be seen as 3D analogues of graphene have attracted enormous interests in research recently. In order to apply these ultrahigh-mobility materials in future electronic/optoelectronic devices, it is crucial to understand the relaxation dynamics of photoexcited carriers and their coupling with lattice. In this work, we report ultrafast transient reflection measurements of the photoexcited carrier dynamics in cadmium arsenide (Cd3As2), which is one of the most stable Dirac semimetals that have been confirmed experimentally. By using low energy probe photon of 0.3 eV, we probed the dynamics of the photoexcited carriers that are Dirac-Fermi-like approaching the Dirac point. We systematically studied the transient reflection on bulk and nanoplate samples that have different doping intensities by tuning the probe wavelength, pump power and lattice temperature, and find that the dynamical evolution of carrier distributions can be retrieved qualitatively by using a two-temperature model. This result is very similar to that of graphene, but the carrier cooling through the optical phonon couplings is slower and lasts over larger electron temperature range because the optical phonon energies in Cd3As2 are much lower than those in graphene.
Ca$^{2+}$ plays an important role in cell signal transduction. Its intracellular propagation is the most basic process of Ca$^{2+}$ signaling, such as calcium wave and double messenger system. In this work, with both numerical simulation and mean field ansatz, the 3-dimensional probability distribution of Ca$^{2+}$, which is read out by phosphorylation, is studied in two scenarios with boundaries. The coverage of distribution of Ca$^{2+}$ is found at an order of magnitude of $mu$m, which is consistent with experimental observed calcium spike and wave. Our results suggest that the double messenger system may occur in the ER-PM junction to acquire great efficiency. The buffer effect of kinase is also discussed by calculating the average position of phosphorylations and free Ca$^{2+}$. The results are helpful to understand the mechanism of Ca$^{2+}$ signaling.
Processes that proceed reliably from a variety of initial conditions to a unique final form, regardless of moderately changing conditions, are of obvious importance in biophysics. Protein folding is a case in point. We show that the action principle can be applied directly to study the stability of biological processes. The action principle in classical physics starts with the first variation of the action and leads immediately to the equations of motion. The second variation of the action leads in a natural way to powerful theorems that provide quantitative treatment of stability and focusing and also explain how some very complex processes can behave as though some seemingly important forces drop out. We first apply these ideas to the non-equilibrium states involved in two-state folding. We treat torsional waves and use the action principle to talk about critical points in the dynamics. For some proteins the theory resembles TST. We reach several quantitative and qualitative conclusions. Besides giving an explanation of why TST often works in folding, we find that the apparent smoothness of the energy funnel is a natural consequence of the putative critical points in the dynamics. These ideas also explain why biological proteins fold to unique states and random polymers do not. The insensitivity to perturbations which follows from the presence of critical points explains how folding to a unique shape occurs in the presence of dilute denaturing agents in spite of the fact that those agents disrupt the folded structure of the native state. This paper contributes to the theoretical armamentarium by directing attention to the logical progression from first physical principles to the stability theorems related to catastrophe theory as applied to folding. This can potentially have the same success in biophysics as it has enjoyed in optics.
Considering a multi-pathway structure in a light-harvesting complex of photosynthesis, we investigate the role of energy-level mismatches between antenna molecules in transferring the absorbed energy to a reaction center. We find a condition in which the antenna molecules faithfully play their roles: Their effective absorption ratios are larger than those of the receiver molecule directly coupled to the reaction center. In the absence of energy-level mismatches and dephasing noise, there arises quantum destructive interference between multiple paths that restricts the energy transfer. On the other hand, the destructive interference diminishes as asymmetrically biasing the energy-level mismatches and/or introducing quantum noise of dephasing for the antenna molecules, so that the transfer efficiency is greatly enhanced to near unity. Remarkably, the near-unity efficiency can be achieved at a wide range of asymmetric energy-level mismatches. Temporal characteristics are also optimized at the energy-level mismatches where the transfer efficiency is near unity. We discuss these effects, in particular, for the Fenna-Matthews-Olson complex.
Previous studies of the flexibilities of ancestral proteins suggests that proteins evolve their function by altering their native state ensemble. Here we propose a more direct method of visualizing this by measuring the changes in the vibrational density of states (VDOS) of proteins as they evolve. Through analysis of VDOS profiles of ancestral and extant proteins we observe that $beta$-lactamase and thioredoxins evolve by altering their density of states in the terahertz region. Particularly, the shift in VDOS profiles between ancestral and extant proteins suggests that nature utilize dynamic allostery for functional evolution. Moreover, we also show that VDOS profile of individual position can be used to describe the flexibility changes, particularly those without any amino acid substitution.
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