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When hydrophobic molecules are solvated in bulk water, possibilities for resolving some of the frustrations in the hydrogen networks appear.
A scenario emerges from these studies in which calcium ions coordinate the structure of interhemichannel hydrophobic domains.
Real proteins have a large " two-letter " component khổng lồ their energy functions, loosely corresponding to lớn hydrophobic- hydrophobic và hydrophobic-hydrophilic interactions.
It was necessary lớn find out whether the binding of hydrophobic compounds occurred lớn other parasites.
Detergents, which are commonly used for stabilizing & purifying hydrophobic molecules, can also be problematic, as detergent micelles scatter very well.
The content of conserved hydrophobic residues in this hairpin is unusually high, & this suggests that the hairpin may interact with a hydrophobic partner.
In addition to the charged amino acids, certain hydrophobic residues appeared to lớn contribute lớn the membrane binding và translocation.
The conserved residues are dominated by glycines & internal hydrophobic amino acids và appear khổng lồ be identical for structural reasons.
The thioredoxin interaction area is different & contains more hydrophobic residues and three histidines one of them very cthua thảm to the active site.
In another possible application, these groups could be part of designed ligands, which may site-specifically penetrate the hydrophobic cores of proteins, possibly inactivating them.
Furthermore, biologically important weak interactions, such as hydrophobic interactions và hydrogen bonding, are weaker at higher temperatures.
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