We provide second- to sixth-order virial coefficients of hard hyperspherocylinders in dependence on their aspect ratio ν. Virial coefficients of an anisotropic geometry in four dimensions are calculated employing an optimized Mayer-sampling algorithm. As the second virial coefficient of a hard particle is identical to its excluded hypervolume, the numerically obtained second virial coefficients can be compared to analytical relations for the excluded hypervolume based on geometric measures of the respective, convex geometry in dependence on its aspect ratio ν.
Nonspecific protein-protein interactions (PPIs) are key to understanding the behavior of proteins in solutions. However, experimentally measuring anisotropic PPIs as a function of orientation and distance has been challenging. Here, we propose to measure a new parameter, the generalized second virial coefficient, (), to address this challenge.
We apply the methodology of Lustig, with which rigorous expressions for all thermodynamic properties can be derived in any statistical ensemble, to derive expressions for the calculation of thermodynamic properties in the path integral formulation of the quantum-mechanical isobaric-isothermal (NpT) ensemble. With the derived expressions, thermodynamic properties such as the density, speed of sound, or Joule-Thomson coefficient can be calculated in path integral Monte Carlo simulations, fully incorporating quantum effects without uncontrolled approximations within the well-known isomorphism between the quantum-mechanical partition function and a classical system of ring polymers. The derived expressions are verified by simulations of supercritical helium above the vapor-liquid critical point at selected state points using recent highly accurate ab initio potentials for pairwise and nonadditive three-body interactions.
Department of Chemistry, James Franck Institute, and Pritzker School of Molecular Engineering, University of Chicago, Chicago, Illinois 60637, United States.
Electrostatically stabilized nanocrystals (NCs) and, in particular, quantum dots (QDs) hold promise for forming strongly coupled superlattices due to their compact and electronically conductive surface ligands. However, studies of the colloidal dispersion and interparticle interactions of electrostatically stabilized sub-10 nm NCs have been limited, hindering the optimization of their colloidal stability and self-assembly. In this study, we employed small-angle X-ray scattering (SAXS) experiments to investigate the interparticle interactions and arrangement of PbS QDs with thiostannate ligands (PbS-SnS) in polar solvents.
We present a method, FMAPS(q), for calculating the structure factor, , of a protein solution, by extending our ast Fourier transform-based odeling of tomistic rotein-protein interactions (FMAP) approach. The interaction energy consists of steric, nonpolar attractive, and electrostatic terms that are additive among all pairs of atoms between two protein molecules. In the present version, we invoke the free-rotation approximation, such that the structure factor is given by the Fourier transform of the protein center-center distribution function .
Sugar molecules play important roles as mediators of biomolecular interactions in cellular functions, disease, and infections. Molecular dynamics simulations are an indispensable tool to explore these interactions at the molecular level. The large time and length scales involved frequently necessitate the use of coarse-grained representations, which heavily depend on the parametrization of sugar-protein interactions.
