Related papers: Dissecting Hydrophobic Hydration and Association
The covalent-like characteristics of hydrogen bonds offer a new perspective on intermolecular interactions. Here, using density functional theory and post-Hartree-Fock methods, we reveal that there are two bonding molecular orbitals (MOs)…
We propose a fully ab initio theory to compute the electron density response under the perturbation in the local field. This method is based on our recently developed local dielectric response theory [Phys. Rev. B 92, 241107(R), 2015],…
The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavourable interactions between hydrophobic residues and water through the formation of a hydrophobic core. Here we include the entropic and enthalpic…
The temperature and length scale dependence of solvation properties of spherical hard solvophobic solutes is investigated in the Jagla liquid, a simple liquid that consists of particles interacting via a spherically symmetric potential…
The phase behavior of colloid-polymer mixtures, and of solutions of globular proteins, is often interpreted in terms of a simple model of hard spheres with short-ranged attraction. While such a model yields a qualitative understanding of…
Molecular dynamics simulations and integral equation calculations of a simple equimolar mixture of diatomic molecules and monomers interacting via attractive and repulsive short-range potentials show the existence of pattern formation…
In order to precisely quantify the fundamental interactions between heterogeneous lipid membranes with coexisting liquid-ordered (Lo) and liquid-disordered (Ld) domains, we performed detailed osmotic stress SAXS experiments by exploiting…
The great challenge with biological membrane systems is the wide range of scales involved, from nanometers and picoseconds for individual lipids, to the micrometers and beyond millisecond for cellular signalling processes. While…
We discuss the simple microscopic derivation of a hydrophobic effect. Our approach is based on the standard functional representation of the partition function of interacting classical particles and subsequent passage to collective…
While individual water molecules adsorb strongly on a talc surface (hydrophilic behavior), a droplet of water beads up on the same surface (hydrophobic behavior). To rationalize this dichotomy, we investigate the influence of the…
Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues tends to occur at the surface of a folded protein. By…
Aqueous solutions of rare gases are studied by computer simulation employing a polarizable potential for both water and solutes. The use of a polarizable potential allows to study the systems from ambient to supercritical conditions for…
The influence of the patchiness and correlations in the distribution of hydrophobic and polar residues at the interface between two rigid biomolecules on their recognition ability is investigated in idealised coarse-grained lattice models.…
Colloidal microgel particles such as poly(N-isopropylacrylamide) (PNIPAM) shrink reversibly in an aqueous medium due to the expulsion of water at a volume phase transition temperature, VPTT $\sim$33$^\circ$C. Romeo et al. [Adv. Mater. 2010,…
We introduce a dissipative particle dynamics scheme for the dynamics of non-ideal fluids. Given a free-energy density that determines the thermodynamics of the system, we derive consistent conservative forces. The use of these effective,…
We consider the hydrodynamic scaling behavior of the mass density with respect to a general class of mass conservative interacting particle systems on ${\mathbb Z}^n$, where the jump rates are asymmetric and long-range of order…
We measure hydrodynamic interactions between colloidal particles confined in a thin sheet of fluid. The reduced dimensionality, compared to a bulk fluid, increases dramatically the range of couplings. Using optical tweezers we force a two…
Hydrogen bonds are a common feature in protein folding and aggregation. Due to their chemical peculiarities in terms of strength and directionality, a particular attention must be paid to the definition of the hydrogen bond potential…
Protein solubility and conformational stability are a result of a balance of interactions both within a protein and between protein and solvent. The electrostatic solvation free energy of oligoglycines, models for the peptide backbone,…
The behavior of proteins near interfaces is relevant for biological and medical purposes. Previous results in bulk show that, when the protein concentration increases, the proteins unfold and, at higher concentrations, aggregate. Here, we…