Related papers: Dynamic Variation in Protein-Small Molecule Intera…
Carefully designed nanostructures can inspire new type of optomechanical interactions and allow surpassing limitations set by classical diffractive optical elements. Apart from strong near-field localization, nanostructured environment…
Trapping cold, chemically important molecules with electromagnetic fields is a useful technique to study small molecules and their interactions. Traps provide long interaction times that are needed to precisely examine these low density…
We report that protein confinement within nanoscopic vesicular compartments corresponds to a liquid-liquid phase transition with the protein/water within vesicle lumen interacting very differently than in bulk. We show this effect leads to…
Protein corona formation and nanoparticle aggregation have been heavily discussed over the last years since the lack of fine-mapping of these two combined effects has hindered the targeted delivery evolution and the personalized…
These lectures will address two questions. Is there a simple variational principle underlying the existence of secondary motifs in the native state of proteins? Is there a general approach which can qualitatively capture the salient…
A microscopic physical analysis of the various resistive effects involved in the electronic detection of single biomolecules in a nanopore of a MoS2 nanoribbon is presented. The analysis relies on a combined experimental-theoretical…
Studies of nanoparticle-based optical matter have only considered spherical constituents. Yet nanoparticles with other shapes are expected to have different local electromagnetic field distributions and therefore interactions with neighbors…
Specific protein-protein interactions are crucial in the cell, both to ensure the formation and stability of multi-protein complexes, and to enable signal transduction in various pathways. Functional interactions between proteins result in…
Many fundamental biological processes are regulated by protein-DNA complexes called {\it synaptosomes}, which possess multiple interaction sites. Despite the critical importance of synaptosomes, the mechanisms of their formation remain not…
Understanding collisions between ultracold molecules is crucial for making stable molecular quantum gases and harnessing their rich internal degrees of freedom for quantum engineering. Transient complexes can strongly influence collisional…
Optical binding interactions between laser-trapped spherical microparticles are familiar in a wide range of trapping configurations. Recently it has been demonstrated that these experiments can be accurately modeled using Mie scattering or…
We study the hydrodynamic coupling of neighboring micro-beads placed in a dual optical trap setup allowing us to precisely control the degree of coupling and directly measure time-dependent trajectories of the entrained beads. Average…
Solving the Bethe-Salpeter equation (BSE) for the optical polarization functions is a first principles means to model optical properties of materials including excitonic effects. One almost ubiquitously used approximation neglects the…
Since the advent of atom laser-cooling, trapping or cooling natural molecules has been a long standing and challenging goal. Here, we demonstrate a method for laser-trapping molecules that is radically novel in its configuration, in its…
An optimization technique is used to determine the pairwise interactions between amino acids in globular proteins. A numerical strategy is applied to a set of proteins for maximizing the native fold stability with respect to alternative…
The optical absorption spectrums of nanomotors made from double-wall carbon nanotubes have been calculated with the time-dependent density functional based tight binding method. When the outer short tube of the nanomotor moves along or…
Protein-DNA interactions are critical for the successful functioning of all natural systems. The key role in these interactions is played by processes of protein search for specific sites on DNA. Although it has been studied for many years,…
Long, flexible physical filaments are naturally tangled and knotted, from macroscopic string down to long-chain molecules. The existence of knotting in a filament naturally affects its configuration and properties, and may be very stable or…
The growing interest for comparing protein internal dynamics owes much to the realization that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional…
Polyphenols and proteins are essential biomolecules that influence food functionality and, by extension, human health. Their interactions -- hereafter referred to as PhPIs (polyphenol-protein interactions) -- affect key processes such as…