Hydrophobic effect in the context of "Protein aggregation"

In chemistry, a non-covalent interaction differs from a covalent bond in that it does not involve the sharing of electrons, but rather involves more dispersed variations of electromagnetic interactions between molecules or within a molecule. The chemical energy released in the formation of non-covalent interactions is typically on the order of 1–5 kcal/mol (1000–5000 calories per 6.02×10 molecules). Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects.

Non-covalent interactions are critical in maintaining the three-dimensional structure of large molecules, such as proteins and nucleic acids. They are also involved in many biological processes in which large molecules bind specifically but transiently to one another (see the properties section of the DNA page). These interactions also heavily influence drug design, crystallinity and design of materials, particularly for self-assembly, and, in general, the synthesis of many organic molecules.

Durable water repellent, or DWR, is a coating added to fabrics at the factory to make them water-resistant (hydrophobic). Most factory-applied treatments are fluoropolymer based; these applications are quite thin and not always effective. Durable water repellents are commonly used in conjunction with waterproof breathable fabrics such as Gore-Tex to prevent the outer layer of fabric from becoming saturated with water. This saturation, called 'wetting out,' can reduce the garment's breathability (moisture transport through the breathable membrane) and let water through. As the DWR wears off over time, re-treatment is recommended when necessary. Many spray-on and wash-in products for treatment of non-waterproof garments and re-treatment of proofed garments losing their water-repellency are available.

Methods for factory application of DWR treatments involve applying a solution of a chemical onto the surface of the fabric by spraying or dipping, or chemical vapor deposition (CVD). The advantages of CVD include reducing the use of environmentally harmful solvents; requiring less DWR; and an extremely thin waterproof layer that has less effect on the natural look and feel of the fabric.

Supramolecular chemistry is the branch of chemistry concerning chemical systems composed of discrete numbers of molecules. The strength of the forces responsible for spatial organization of the system ranges from weak intermolecular forces, electrostatic charge, or hydrogen bonding to strong covalent bonding, provided that the electronic coupling strength remains small relative to the energy parameters of the component. While traditional chemistry concentrates on the covalent bond, supramolecular chemistry examines the weaker and reversible non-covalent interactions between molecules. These forces include hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi–pi interactions and electrostatic effects.

Important concepts advanced by supramolecular chemistry include molecular self-assembly, molecular folding, molecular recognition, host–guest chemistry, mechanically-interlocked molecular architectures, and dynamic covalent chemistry. The study of non-covalent interactions is crucial to understanding many biological processes that rely on these forces for structure and function. Biological systems are often the inspiration for supramolecular research.

In chemistry, folding is the process by which a molecule assumes its shape or conformation. The process can also be described as intramolecular self-assembly, a type of molecular self-assembly, where the molecule is directed to form a specific shape through noncovalent interactions, such as hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi-pi interactions, and electrostatic effects.

The most active area of interest in the folding of molecules is the process of protein folding, which analyses the specific sequences of amino acids in a protein. The shape of the folded protein can be used to understand its function and design drugs to influence the processes that it is involved in.