Forces also hydrogen bonding

When thinking about chemical reactivity, chemists usually focus their attention on bonds, the covalent interactions between atoms within individual molecules. Also important, hotvever, particularly in large biomolecules like proteins and nucleic acids, are a variety of interactions between molecules that strongly affect molecular properties. Collectively called either intermolecular forces, van der Waals forces, or noncovalent interactions, they are of several different types dipole-dipole forces, dispersion forces, and hydrogen bonds. 

There are three types of nonbonding intermolecular interaction dipole-dipole interactions, van der Waals forces and hydrogen bonding. These interactions increase significantly as the molecular weights increase, and also increase with increasing polarity of the molecules. 

In this section, we explore how water molecules in the liquid phase interact with one another via cohesive forces, which are forces of attraction between molecules of a single substance. For water, the cohesive forces are hydrogen bonds. We also explore how water molecules interact with other polar materials, such as glass, through adhesive forces, forces of attraction between molecules of two different substances. 

A substrate binds an enzyme at the active site. Substrate-enzyme binding is based on weak intermolecular attractions contact forces, dipole forces, and hydrogen bonding. Steric effects also play an important role because the substrate must physically fit into the active site. Some enzymes have confined active sites, while others are open and accessible. A restricted active site can lead to high selectivity for a specific substrate. Low specificity can be advantageous for some enzymes, particularly metabolic and digestive enzymes that need to process a broad range of compounds with a variety of structures. Because enzymes are composed of chiral amino acids, enzymes interact differently with stereoisomers, whether diastereomers or enantiomers. 

These principles are best recognized when studying relatively simple molecular systems that have an ability to exploit weak interactions to create structure. Among many, peptides are the perfect choice for such studies considering their versatility in make up given the 20+ natural and synthetic amino acid residues, and their functional diversity. In addition, the amino acid sequence of the primary structure combined with the ability of forming secondary (3-sheet or a-helix structures provide substantial room for the creation of hierarchical structures based on weak intermolecular forces, mainly hydrogen bonds. A limited sequence of residues also prevents additional complication from tertiary and quaternary structures as seen with proteins. 

A second limitation of the Hughes-Ingold theory concerns the fact that the solvent is treated as dielectric continuum, characterized by one of the following its relative permittivity, e, the dipole moment, fi, or by its electrostatic factor, EF, defined as the product of and [27]. The term solvent polarity refers then to the ability of a solvent to interact electrostatically with solute molecules. It should be remembered, however, that solvents can also interact with solute molecules through specific inter-molecular forces like hydrogen bonding or EPD/EPA complexation cf. Section 2.2). For example, specific solvation of anionic solutes by pro tic solvents may reduce their nucleophilic reactivity, whereas in dipolar aprotic solvents solvation of anions is less,... 

As the data for the Menschutkin reactions indicate, the character of the solute-solvent interactions is more complex than described by Eq. (5-87). It is evident that functions of relative permittivity alone, as given in Eq. (5-87), are not useful for describing the solvent effect on reactions between dipolar reactants, except in certain special cases, such as when a mixture of two solvents is used. In addition to electrostatic forces, non-electrostatic interactions, such as dispersion forces and hydrogen-bonding, must also be involved in Menschutkin reactions. 

The three intermolecular forces are dipolar attractions, van der Waals forces (also called London forces), and hydrogen bonding. The effects of dipoles (Section 13.5) are considered first, followed by discussions of van der Waals forces and hydrogen bonding. 

In a solution, nanoparticles interact with each other in a number of ways. Widely separated nanoparticles may be brought into contact by Brownian motion. As they approach each other, electrostatic, van der Waals forces, and hydrogen bonding, in addition to Brownian motion, can cause two nanoparticles to rotate with respect to each other, and collide. Evidently, under some conditions, the collisions that result in fusion are those that involve two nanoparticles in appropriate orientations to form a coherent (or semicoherent) interface. Particle rotation in the absence of a fluid has been modeled computationally (Zhu and Averback 1996), implying that oriented assembly-based crystal growth can also occur in dry systems. 

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