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Hydrophilic interaction chromatography (or hydrophilic interaction liquid chromatography, HILIC) [1] is a variant of normal phase liquid chromatography that partly overlaps with other chromatographic applications such as ion chromatography and reversed phase liquid chromatography. HILIC uses hydrophilic stationary phases with reversed-phase ...
A hydrophilic molecule or portion of a molecule is one whose interactions with water and other polar substances are more thermodynamically favorable than their interactions with oil or other hydrophobic solvents. [2] [3] They are typically charge-polarized and capable of hydrogen bonding.
where C R (>0) is a measure of the hydration interaction energy for hydrophilic molecules of the given system, λ R is a characteristic length scale of hydration repulsion and z is the distance of separation. In other words, it is on distances up to this length that molecules/surfaces fully experience this repulsion.
Pages for logged out editors learn more. Contributions; Talk; Hydrophilic interaction liquid chromatography
This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains.
The energetics of DNA tertiary-structure assembly were determined to be driven by the hydrophobic effect, in addition to Watson–Crick base pairing, which is responsible for sequence selectivity, and stacking interactions between the aromatic bases.
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 ...
In this case, the hydrophilic groups are sequestered in the micelle core and the hydrophobic groups extend away from the center. These inverse micelles are proportionally less likely to form on increasing headgroup charge, since hydrophilic sequestration would create highly unfavorable electrostatic interactions.