The so-called island model of protein structural transition holds that hydrophobic interactions are the key to both the folding and function of proteins. Herein, the genesis and statistical mechanical basis of the island model of transitions are reviewed, by presenting the results of simulations of such transitions. Elucidating the physicochemical mechanism of protein structural formation is th...

In the current work, we demonstrate how coordination chemistry can be employed to direct self-assembly based on strong hydrophobic interactions. To investigate the influence of coordination sphere geometry on aqueous self-assembly, we synthesized complexes of the amphiphilic perylene diimide terpyridine ligand with the first-row transition-metal centers (zinc, cobalt, and nickel). In aqueous me...

The principles obtained from studies on molecular chaperones have provided explanations for the assisted protein folding in vivo. However, the majority of proteins can fold without the assistance of the known molecular chaperones, and little attention has been paid to the potential chaperoning roles of other macromolecules. During protein biogenesis and folding, newly synthesized polypeptide ch...

In the present work, we have explored the use of the triphenylmethyl group, a commonly used protecting group for primary alcohols as a gelling structural component in the design of molecular gelators. We synthesized a small library of triphenylmethyl derivatives of simple primary alcohols and studied their gelation properties in different solvents. Gelation efficiency for some of the derivative...

The interaction between two associating hydrophobic particles has traditionally been explained in terms of the release of entropically frustrated hydration shell water molecules. However, this picture cannot account for the kinetics of hydrophobic association and is therefore not capable of providing a microscopic description of the hydrophobic interaction (HI). Here, Monte Carlo simulations of...

in the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (bsa) have been analyzed on basis of intrinsic thermodynamic quantities. in this regards, the intrinsic gibbs free energy of binding, agb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...

The influence of pH on the sorption of pentachlorophenol (PCP) onto three organic amendments, char, humic acid (HA) and peat, and the effect of organic amendments on PCP sorption to three kinds of soils were evaluated. The sorption of PCP on these sorbents fitted the Freundlich model well, suggesting that PCP sorption isotherms were nonlinear with exponential coefficient (N) value lower than 1....

In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, altho...

A combination of atomic force microscopy (AFM) and reflection interference contrast microscopy (RICM) was used to measure simultaneously the interaction force and the spatiotemporal evolution of the thin water film between a bubble in water and mica surfaces with varying degrees of hydrophobicity. Stable films, supported by the repulsive van der Waals-Casimir-Lifshitz force were always observed...

Unspecific adhesion of bacteria is usually the first step in the formation of biofilms on abiotic surfaces, yet it is unclear up to now which forces are governing this process. Alongside long-ranged van der Waals and electrostatic forces, short-ranged hydrophobic interaction plays an important role. To characterize the forces involved during approach and retraction of an individual bacterium to...