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The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute, causing the water to compensate by forming a clathrate-like cage structure around the non-polar molecules. This structure is more highly ordered than free water ...
The hydrophobic effect is the observed tendency of nonpolar ... Some argue that the hydrophobic interaction is mostly an entropic effect originating from the ...
Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects. [3] [2] Non-covalent interactions [4] are critical in maintaining the three-dimensional structure of large molecules, such as proteins and nucleic acids.
[7] [9] Hydrophobic molecules can be eluted from the column by decreasing the polarity of the mobile phase using an organic (non-polar) solvent, which reduces hydrophobic interactions. The more hydrophobic the molecule, the more strongly it will bind to the stationary phase, and the higher the concentration of organic solvent that will be ...
Host–guest chemistry encompasses the idea of molecular recognition and interactions through non-covalent bonding. Non-covalent bonding is critical in maintaining the 3D structure of large molecules, such as proteins and is involved in many biological processes in which large molecules bind specifically but transiently to one another.
Initially, the interaction between the active site and the substrate is non-covalent and transient. There are four important types of interaction that hold the substrate in a defined orientation and form an enzyme-substrate complex (ES complex): hydrogen bonds, van der Waals interactions, hydrophobic interactions and electrostatic force ...
A chaotropic agent is a substance which disrupts the structure of, and denatures, macromolecules such as proteins and nucleic acids (e.g. DNA and RNA).Chaotropic solutes increase the entropy of the system by interfering with intermolecular interactions mediated by non-covalent forces such as hydrogen bonds, van der Waals forces, and hydrophobic effects.
The protein–protein interactions thus become stronger than the solvent–solute interactions and the protein molecules associate by forming hydrophobic interactions with each other. [5] After dissociation in a given solvent, the negatively charged atoms from a chosen salt begin to compete for interactions with positively charged molecules ...