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Hydrophobic interaction

Main driving forces of protein folding
synonym Hydrophobic effect (Hydrophobic effect) generally refers to hydrophobic interaction
sparse water The interaction is protein folding Main points of drive Hydrophobic group The phenomenon of gathering close to each other to avoid boiling water is called hydrophobic interaction. When protein Drainage in Side chain Aggregating protein Quality inside, not by water solvent The protein is very stable in water. Hydrophobic interactions play a major role in maintaining protein conformation, because water molecules interact with each other more than water with other molecules Nonpolar molecule The effect of is stronger. The non-polar side chains aggregate inside the protein molecules to avoid boiling water. At the same time, most polar side chains maintain contact with water on the protein surface. The hydrophobic properties within the molecule not only explain the hydrophobic Residue It also shows the stability of spiral and folded sheet. [1]
Chinese name
Hydrophobic interaction
Foreign name
hydrophobic interaction
Alias
Hydrophobic interaction
Nature
Weak, noncovalent interactions
interpretation
Hydrophobic interaction occurs through the mutual repulsion between hydrophobic groups of hydrophobic substances and water, and hydrophobic groups are generally non-polar groups. This action makes the hydrophobic groups close to each other, and at the same time makes the water concentrated and more structured.
cage hydrate An image formed by hydrophobic interaction dry ice That way Inclusion compound The "master" substance, i.e. water, forms a cage like structure through hydrogen bonding, which physically traps a "guest" substance, i.e. small hydrophobic molecules. Cage hydrates represent the largest structural response of water to a non-polar substance, similar to Microstructure It also naturally exists in biological substances.
Hydrophobic interactions affect most protein The structure and nature of is critical. Hydrophobic interactions provide the main impetus , drain water Residue It is located inside the protein molecule. Interestingly, although most hydrophobic groups of proteins aggregate due to hydrophobic interactions, about 1/3 of hydrophobic groups are still exposed to water, so the special structure of water on the hydrophobic surface exists in the hydration structure of proteins. Lowering the temperature weakens the hydrophobic interaction and strengthens the hydrogen bond.
The interaction length of hydrophobic interaction can reach about 100 nm, while other molecules Force Only about 5 nm at most. However, the hydrophobic interaction is so long Operating distance Up to now, scientists have not reached a satisfactory conclusion in their research on the subject.