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The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. [19] The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. [3]
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 ...
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.
Schematic representation of the different types of interaction between monotopic membrane proteins and the cell membrane: 1. interaction by an amphipathic α-helix parallel to the membrane plane (in-plane membrane helix) 2. interaction by a hydrophobic loop 3. interaction by a covalently bound membrane lipid (lipidation) 4. electrostatic or ...
Hydrophobic interactions are essentially entropic interactions basically due to order/disorder phenomena in an aqueous medium. The free energy associated with minimizing interfacial areas is responsible for minimizing the surface area of water droplets and air bubbles in water.
The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]
Host-guest interaction has raised dramatical attention since it was discovered. It is an important field, because many biological processes require the host-guest interaction, and it can be useful in some material designs. There are several typical host molecules, such as, cyclodextrin, crown ether, et al.
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.