The hydrophobic interaction drives nonpolar solutes to aggregate in aqueous solution, and hence plays a critical role in many fundamental processes in nature. An important property intrinsic to hydrophobic interaction is its cooperative nature, which is originated from the collective motions of water hydrogen bond networks surrounding hydrophobic solutes. This property is widely believed to enh...

Hydrophobic interactions constitute one of the most important types of nonspecific interactions in biological systems, which emerge when water molecules rearrange as two hydrophobic species come close to each other. The prediction of hydrophobic interactions at the level of nanoparticles (Brownian objects) remains challenging because of uncontrolled diffusive motion of the particles. We describ...

A three dimensional model of the basic Helix-Loop-Helix motif and its sequence specific recognition of DNA is described. The basic-helix I is modeled as a continuous ?-helix because no ?-helix breaking residue is found between the basic region and the first helix. When the basic region of the two peptide monomers are aligned in the successive major groove of the cognate DNA, the hydrophobi...

We review some results concerning the energetic and dynamical consequences of taking a generic hydrophobic model of a random polypeptide chain, where the effective hydrophobic interactions are represented by Hookean springs. Then we present a set of calculations on a microscopic model of hydrophobic interactions, investigating the behaviour of a hydrophobic chain in the vicinity of a hydrophobi...

Fundamental studies of the effect of specific ions on hydrophobic interactions are driven by the need to understand phenomena such as hydrophobically driven self-assembly or protein folding. Using β-peptide-inspired nanorods, we investigate the effects of both free ions (dissolved salts) and proximally immobilized ions on hydrophobic interactions. We find that the free ion effect is correlated ...

UV-visible and Fluorescence spectroscopic methods were employed to study the interaction of human serum albumin (HSA) with Valacyclovir Hydrochloride. Additionally, molecular dynamics and molecular docking simulations were used to visualize and specify the binding site of Valacyclovir Hydrochloride. The Stern-Volmer and van't Hoff equations along with spectroscopic observations, were used to de...

curcumin (cur) is the active curcuminoid with many physiological, biochemical, and pharmacological properties. solubility and stability of cur is the limiting factors for realizing its therapeutic potential. bovine β-casein is an abundant milk protein that is highly amphiphilic and self-assembles into stable micellar nanoparticles in aqueous solution. β-casein nanoparticle can solubilize cur mo...

human serum albumin (hsa) is the most abundant protein constituent of blood plasma. this protein consists of a single polypeptide chain of 585 amino acid residues, which has many important physiological functions. hsa can bind and carry many drugs, including anticoagulants, tranquilizers, and general anesthetics. some technique such as: fluorescence spectroscopy, three-dimensional fluorescence ...

The binding data for interaction of a homologous series of n-alkyl sulfates with alkyl chainlengths from C8 to C12 with insulin were analyzed on basis of Hill equation for two classes ofbinding sites .The intrinsic Gibbs free energies were calculated and resolute on basis ofelectrostatic and hydrophobic contributions The estimation of these contributions reveals themajor role of electrostatic i...