Bandwidth tunability of graphene absorption enhancement by hybridization of delocalized surface plasmon polaritons and localized magnetic plasmons.

The bandwidth-tunable absorption enhancement of monolayer graphene is theoretically studied in the near-infrared wavelengths. The monolayer graphene is placed on the silver substrate surface with a periodic array of one-dimensional slits. Two absorption peaks are found to result from the hybridization of delocalized surface plasmon polaritons and localized magnetic plasmons. The positions of absorption peaks are accurately predicted by a coupling model of double oscillators. The full width at half maximum of absorption peaks is largely tuned from about 1-200 nm by changing the array period of slits. The effect of the slit size on absorption peaks is also investigated in detail. Our work is promising in applications for photoelectric devices.

Landscape-Based View on the Stepping Movement of Myosin VI.

Myosin VI dimer walks toward the minus end of the actin filament with a large and variable step size of 25-36 nm. Two competing models have been put forward to explain this large step size. The Spudich model assumes that the myosin VI dimer associates at a distal tail near the cargo-binding domain, which makes two full-length single α-helix (SAH) domains serve as long legs. In contrast, the Houdusse-Sweeney model assumes that the association occurs in the middle (between residues 913 and 940) of the SAH domain and that the three-helix bundles unfold to ensure the large step size. Their consistency with the observation of stepping motion with a large and variable step size has not been examined in detail. To compare the two proposed models of myosin VI, we computationally characterized the free energy landscape experienced by the leading head during the stepping movement along the actin filament using the elastic network model of two heads and an implicit model of the SAH domains. Our results showed that the Spudich model is more consistent with the 25-36 nm step size than the Houdusse-Sweeney model. The unfolding of the three-helix bundles gives rise to the free energy bias toward a shorter distance between two heads. Besides, the stiffness of the SAH domain is a key factor for giving strong energetic bias toward the longer distance of stepping. Free energy analysis of the stepping motion complements the visual inspection of static structures and enables a deeper understanding of underlying mechanisms of molecular motors.

Effects of electrostatic interactions on global folding and local conformational dynamics of a multidomain Y-family DNA polymerase.

The Y-family DNA polymerases specialize in translesion DNA synthesis, which is essential for replicating damaged DNA. The Y-family polymerases, which are made up of four stable domains, exhibit extensive distributions of charged residues, and are responsible for the tight formation of the protein-DNA complex. However, it is still unclear how the electrostatic interactions influence the conformational dynamics of the polymerases. Here, we focus on the case of a prototype Y-family DNA polymerase, Dpo4. Using coarse-grained models including a salt-dependent electrostatic potential, we investigate the effects of the electrostatic interactions on the folding process of Dpo4. Our simulations show that strong electrostatic interactions result in a three-state folding of Dpo4, consistent with the experimental observations. This folding process exhibits low cooperativity led by low salt concentration, where the individual domains fold one by one through one single pathway. Since the refined folding order of domains in multidomain proteins can shrink the configurational space, we suggest that the electrostatic interactions facilitate the Dpo4 folding. In addition, we study the local conformational dynamics of Dpo4 in terms of fluctuation and frustration analyses. We show that the electrostatic interactions can exaggerate the local conformational properties, which are in favor of the large-scale conformational transition of Dpo4 during the functional DNA binding. Our results underline the importance of electrostatic interactions in the conformational dynamics of Dpo4 at both the global and local scale, providing useful guidance in protein engineering at the multidomain level.

Randomness of Eigenstates of Many-Body Quantum Systems.

The emergence of random eigenstates of quantum many-body systems in integrable-chaos transitions is the underlying mechanism of thermalization for these quantum systems. We use fidelity and modulus fidelity to measure the randomness of eigenstates in quantum many-body systems. Analytic results of modulus fidelity between random vectors are obtained to be a judge for the degree of randomness. Unlike fidelity, which just refers to a kind of criterion of necessity, modulus fidelity can measure the degree of randomness in eigenstates of a one-dimension (1D) hard-core boson system and identifies the integrable-chaos transition in this system.

Photovoltage Reversal in Organic Optoelectronic Devices with Insulator-Semiconductor Interfaces.

Photoinduced space-charges in organic optoelectronic devices, which are usually caused by poor mobility and charge injection imbalance, always limit the device performance. Here we demonstrate that photoinduced space-charge layers, accumulated at organic semiconductor-insulator interfaces, can also play a role for photocurrent generation. Photocurrent transients from organic devices, with insulator-semiconductor interfaces, were systematically studied by using the double-layer model with an equivalent circuit. Results indicated that the electric fields in photoinduced space-charge layers can be utilized for charge generation and can even induce a photovoltage reversal. Such an operational process of light harvesting would be promising for photoelectric conversion in organic devices.

Coupling of lever arm swing and biased Brownian motion in actomyosin.

An important unresolved problem associated with actomyosin motors is the role of Brownian motion in the process of force generation. On the basis of structural observations of myosins and actins, the widely held lever-arm hypothesis has been proposed, in which proteins are assumed to show sequential structural changes among observed and hypothesized structures to exert mechanical force. An alternative hypothesis, the Brownian motion hypothesis, has been supported by single-molecule experiments and emphasizes more on the roles of fluctuating protein movement. In this study, we address the long-standing controversy between the lever-arm hypothesis and the Brownian motion hypothesis through in silico observations of an actomyosin system. We study a system composed of myosin II and actin filament by calculating free-energy landscapes of actin-myosin interactions using the molecular dynamics method and by simulating transitions among dynamically changing free-energy landscapes using the Monte Carlo method. The results obtained by this combined multi-scale calculation show that myosin with inorganic phosphate (Pi) and ADP weakly binds to actin and that after releasing Pi and ADP, myosin moves along the actin filament toward the strong-binding site by exhibiting the biased Brownian motion, a behavior consistent with the observed single-molecular behavior of myosin. Conformational flexibility of loops at the actin-interface of myosin and the N-terminus of actin subunit is necessary for the distinct bias in the Brownian motion. Both the 5.5-11 nm displacement due to the biased Brownian motion and the 3-5 nm displacement due to lever-arm swing contribute to the net displacement of myosin. The calculated results further suggest that the recovery stroke of the lever arm plays an important role in enhancing the displacement of myosin through multiple cycles of ATP hydrolysis, suggesting a unified movement mechanism for various members of the myosin family.

Conformational flexibility of loops of myosin enhances the global bias in the actin-myosin interaction landscape.

A long-standing controversy on the mechanism of an actomyosin motor is the role of the Brownian motion of the myosin head in force generation. In order to shed light on this problem, we calculate free-energy landscapes of interaction between an actin filament and the head (S1) of myosin II by using a coarse-grained model of actomyosin. The results show that the free-energy landscape has a global gradient toward the strong-binding site on actin filament, which explains the biased Brownian motion of myosin S1 observed in a single-molecule experiment [Kitamura et al., Nature, 1999, 397, 129 and Biophysics, 2005, 1, 1]. The distinct global gradient in the landscape is brought about only when the conformation of loop 2 at the actin interface of myosin S1 is flexible. The conformational flexibility of loop 3 also contributes to the gradient in the landscape by compensating the role of loop 2. Though the structure of loop 2 is expanded in the weak-binding state, loop 2 shows the larger fluctuation of compaction and expansion due to the actin-myosin interactions as myosin S1 moves toward the strong-binding site on actin filament. Hence, the increase in the compaction-expansion fluctuation of loop 2, the stronger binding of myosin to actin, and the biased Brownian motion of myosin S1 are coupled with each other and should take place in a concurrent way. This predicted coupling should provide opportunities to further test the hypothesis of the biased Brownian motion in actomyosin.