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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 ...
Just as in hydrophilic interaction chromatography (HILIC; a sub-technique within HPLC), this method separates analytes based on differences in their polarity. HILIC most often uses a bonded polar stationary phase and a mobile phase made primarily of acetonitrile with water as the strong component. Partition HPLC has been used historically on ...
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In 1986, Regnier’s group synthesized a stationary phase that had characteristics of anion exchange chromatography (AEX) and hydrophobic interaction chromatography (HIC) on protein separation. [8] In 1998, a new form of MMC, hydrophobic charge induction chromatography (HCIC), was proposed by Burton and Harding.
Pliska and his coworkers [27] used thin layer chromatography to relate mobility values of free amino acids to their hydrophobicities. About a decade ago, another hydrophilicity scale was published, this scale used normal phase liquid chromatography and showed the retention of 121 peptides on an amide-80 column. [ 28 ]
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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]
Hence, non-polar solutes tend not to be soluble in polar solvents because these solvent-solvent binding interactions must be overcome first. When applied to liquid chromatography (LC), solvophobic theory attributes the retention of solutes on the stationary phase partly to the rejection of solute molecules by the solvent, and partly to the ...