Similarities Between Van Der Waals, Electrostatic, Hydrogen Bonding and Hydrophobic

It is true that the hydrogen bonds between water molecules will be broken when a hydrophobe is introduced into an aqueous medium; however, hydrophobes do not interact with water molecules in any way. Because breaking bonds results in the introduction of heat into the system, this process is classified as an endothermic reaction.

Bonding with Hydrogen 

Many of water’s vital, life-sustaining characteristics are provided by hydrogen bonding, which also serve to stabilise the structures of proteins and DNA, the cellular building block. Because hydrogen’s one electron is drawn more strongly toward the other element and away from the hydrogen when polar covalent bonds involving hydrogen form, the hydrogen in those bonds has a little positive charge. The hydrogen will be drawn to nearby negative charges since it is somewhat positive. When this happens, the – charge on the more electronegative atoms of another molecule, usually oxygen or nitrogen, or within the same molecule, interacts with the + charge on the hydrogen from one molecule. A hydrogen bond refers to this interaction. Water molecules frequently form this type of connection. Individual hydrogen bonds are weak and easily broken; but, they are abundant in water and organic polymers, where they combine to create a powerful force. The DNA double helix is held together by hydrogen bonds as well.

Hydrogen Bonding’s Applications 

Inorganic materials like water and organic compounds like DNA and proteins both have hydrogen bonds. Hydrogen bonding between complementary nucleotides keeps DNA’s two strands together (A&T, C&G).  Water’s high boiling point (100 °C) and surface tension are attributed to hydrogen bonding. 

The hydrogen bonds created between water molecules in water droplets are stronger than the other intermolecular forces between the water molecules and the leaf, contributing to high surface tension and distinct water droplets. 

The secondary, tertiary, and quaternary structures of proteins and nucleic acids are partially due to intramolecular hydrogen bonding in biology. Proteins and nucleic acids may develop and maintain certain structures thanks to hydrogen bonding. 

Interactions of the Van der Waals Type 

Van der Waals interactions, like hydrogen bonds, are weak molecular interactions. Van der Waals attractions can happen between any two or more molecules and are caused by minor changes in electron concentrations, which are not always symmetrical around an atom. The molecules must be quite close to one another for these interactions to occur. These connections, along with ionic, covalent, and hydrogen bonds, let proteins achieve their three-dimensional structure, which is required for proper function. 

In gases, liquefied and solidified gases, and practically all organic liquids and solids, van der Waals forces attract neutral molecules to one another. The intermolecular forces are named after Dutch physicist Johannes Diderik van der Waals, who proposed them in 1873 as part of a theory to explain the behaviour of actual gases. Van der Waals forces hold solids together, so they have lower melting points and are softer than ionic, covalent, and metallic bonds. 

Three types of Van der Waals forces can exist. For starters, some materials’ molecules may be permanent electric dipoles, despite being electrically neutral. One side of a molecule is always somewhat positive, and the opposite side is always somewhat negative, due to a fixed distortion in the distribution of electric charge in the very structure of some molecules. The tendency for permanent dipoles to align with one another produces a net attractive force. Second, the presence of permanent dipole molecules causes the electron charge in nearby polar or nonpolar molecules to be temporarily distorted, causing further polarisation. When a permanent dipole interacts with a nearby induced dipole, it produces an additional attractive force. Third, even if no molecules of a material are permanent dipoles (as in the noble gas argon or the organic liquid benzene), there is a force of attraction between them, which accounts for condensing to the liquid state at sufficiently low temperatures. 

Fritz London, a Polish-born physicist, was the first to recognise the nature of this attractive force in molecules, which requires quantum mechanics to accurately describe. The centre of negative charge of electrons and the centre of positive charge of atomic nuclei are unlikely to coincide at any given time, according to London. Even though the average of this instantaneous polarisation over a brief time interval may be zero, the fluctuation of electrons causes molecules to be time-varying dipoles. Such time-varying dipoles, also known as instantaneous dipoles, are unable to align themselves to account for the actual force of attraction, but they do induce properly aligned polarisation in adjacent molecules, resulting in attractive forces. Even between permanently polar molecules, these specific interactions, or forces, arising from electron fluctuations in molecules (known as London forces, or dispersion forces), are present and contribute the most to intermolecular forces. 

Interactions between Hydrophobic Molecules and Hydrogen Atoms 

The relationship between water and hydrophobes is known as hydrophobic interactions (low water-soluble molecules). Nonpolar hydrophobic have a long carbon chain that does not interact with water molecules. A good example of this interaction is when fat and water are mixed together. Water and fat do not mix, according to popular belief, because the Van der Waals forces acting on both water and fat molecules are too weak. This is not the case, however. The intermolecular forces of a fat droplet in water are less important than the reaction’s enthalpy and entropy. 

Hydrophobic Interactions and Their Causes 

Nonpolar substances like fat molecules clump up together rather than distributing themselves in a water medium, according to American chemist Walter Kauzmann, because this allows the fat molecules to have minimal contact with water. 

The Importance of Hydrophobic Interactions in Biology 

Hydrophobic interactions are crucial for protein folding. This is critical for maintaining a protein stable and biologically active because it allows the protein’s surface area to decrease, reducing unwanted water interactions. Aside from proteins, many other biological substances, such as phospholipid bilayer membranes in every cell of your body, rely on hydrophobic interactions for survival and function.

Conclusion

From the following article we can conclude that Hydrogen bonds between water molecules are disrupted when a hydrophobe is dropped in an aqueous solution, but water molecules do not react with the hydrophobe. Because heat is introduced into the system when bonds are broken, this is an endothermic reaction.