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The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water. [ 1 ] [ 2 ] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact ...
The hydrophobic effect represents the tendency of water to exclude non-polar molecules. The effect originates from the disruption of highly dynamic hydrogen bonds between molecules of liquid water. Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect.
The hydrophobic effect is the phenomenon in which the hydrophobic chains of a protein collapse into the core of the protein (away from the hydrophilic environment). [12] In an aqueous environment, the water molecules tend to aggregate around the hydrophobic regions or side chains of the protein, creating water shells of ordered water molecules ...
Biochemistry, or biological chemistry, is the study of chemical processes within and relating to living organisms. [1] A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at ...
The hydrophobic effect is the desire for non-polar molecules to aggregate in aqueous solutions in order to separate from water. [22] This phenomenon leads to minimum exposed surface area of non-polar molecules to the polar water molecules (typically spherical droplets), and is commonly used in biochemistry to study protein folding and other ...
When the solvent is water, this is known as the hydrophobic effect. Alternatively, the binding may be enthalpy -driven where non-covalent attractive forces such as electrostatic attraction, hydrogen bonding , and van der Waals / London dispersion forces are primarily responsible for the formation of a stable complex. [ 11 ]
Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...
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 ...