Related papers: Dynamic Variation in Protein-Small Molecule Intera…
A major impediment to a more complete understanding of barrier crossing and other single-molecule processes is the inability to directly visualize the trajectories and dynamics of atoms and molecules in reactions. Rather, the kinetics are…
Reaction dynamics involving subdiffusive species is an interesting topic with only few known results, especially when the motion of different species is characterized by different anomalous diffusion exponents. Here we study the reaction…
The dynamics of motor protein molecules that have two subunits is investigated using simple discrete stochastic models. Exact steady-state analytical expressions are obtained for velocities and dispersions for any number of intermediate…
The size of particles which can be trapped in optical tweezers ranges from tens of nanometres to tens of micrometres. This size regime also includes large single molecules. Here we present experiments demonstrating that optical tweezers can…
In the last years, it was demonstrated that neutral molecules can be loaded on a microchip directly from a supersonic beam. The molecules are confined in microscopic traps that can be moved smoothly over the surface of the chip. Once the…
The interactions of a protein, its phase behavior, and ultimately, its ability to function, are all influenced by the interactions between the protein and its hydration waters. Here we study proteins with a variety of sizes, shapes,…
The interaction of light with photosynthetic proteins is an extremely efficient process and has been thoroughly investigated. However, exploring light-matter interactions in hybrid nano-solid-photosynthetic proteins is a relatively new and…
We present a simple model of protein folding dynamics that captures key qualitative elements recently seen in all-atom simulations. The goals of this theory are to serve as a simple formalism for gaining deeper insight into the physical…
We demonstrate the realization of (laterally) optically bounded colloidal structures on a liquid-liquid interface of an emulsion droplet. We use DNA tethers to graft the particles to the droplet surface, effectively confining them to a…
Optically levitated multiple nanoparticles has emerged as a platform for studying complex fundamental physics such as non-equilibrium phenomena, quantum entanglement, and light-matter interaction, which could be applied for sensing weak…
We investigate the dynamics of nanoscale droplets in the vicinity of chemical steps which separate parts of a substrate with different wettabilities. Due to long-ranged dispersion forces, nanodroplets positioned on one side of the step…
Much of the complexity observed in gene regulation originates from cooperative protein-DNA binding. While studies of the target search of proteins for their specific binding sites on the DNA have revealed design principles for the…
Optically levitated dielectric nanoparticles have become valuable tools for precision sensing and quantum optomechanical experiments. To predict the dynamic properties of a particle trapped in an optical tweezer with high fidelity, a tool…
A low-temperature dynamical transition has been reported in several proteins. We provide the first observation of a `protein-like' dynamical transition in nonbiological aqueous environments. To this aim we exploit the popular colloidal…
A new trap for atoms and small particles based on the interaction between an atom and the field of counter-propagating light pulses that are partially superposed in time has been proposed. A substantial difference from the known analogs…
We develop coarse-grained models that describe the dynamic encapsidation of functionalized nanoparticles by viral capsid proteins. We find that some forms of cooperative interactions between protein subunits and nanoparticles can…
Protein dynamics has been investigated on a wide range of time scales. Nano- and picosecond dynamics have been assigned to local fluctuations, while slower dynamics have been attributed to larger conformational changes. However, it is…
Proteins need to selectively interact with specific targets among a multitude of similar molecules in the cell. But despite a firm physical understanding of binding interactions, we lack a general theory of how proteins evolve high…
We describe, at the microscopic level, the dynamics of N interacting components where the probability is very small when N is large that a given component interact more than once, directly or indirectly, up to time t, with any other…
Receptor-ligand interactions are essential for biological function and their binding strength is commonly explained in terms of static lock-and-key models based on molecular complementarity. However, detailed information of the full…