hydrophobic

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Related to Hydrophobic interaction: Hydrophobic Interaction Chromatography

hydrophobic

[¦hī·drə′fō·bik]
(chemistry)
Lacking an affinity for, repelling, or failing to adsorb or absorb water.
(medicine)
Of, pertaining to, or suffering from hydrophobia.
References in periodicals archive ?
In the process of simulation, the conformation of tyramine changed and a mass of water molecules formed a hydrogen bonds grid surrounded tyramine, solvated it and weakened its hydrophobic interactions due to its good hydrophilic nature.
Several authors verified hydrophobic interactions, especially in proteins with greater rates of proline (Baxter, Lilley, Haslam & Williamson, 1997; Charlton et al.
Based upon current evidence, this process includes both hydrophobic interactions and hydrogen bonding, with the bottom line effect being that tannin likes to "stick" to protein.
Johansson; Gradient and isocratic high--performance hydrophobic interaction chromatography of proteins on agarose columns.
The hydrophobicity of the cell surface is important in adhesion because hydrophobic interactions tend to increase with an increasing nonpolar nature of one or both surfaces involved (i.
It offers LC media and columns for reversed phase, ion exchange, hydrophobic interaction, gel filtration, and affinity separations and K-Prime 40 Biochromatography systems for process LC.
The contribution of electrostatic and hydrophobic interaction to the stability of proteins and other supramolecular structures will also be analyzed.
Laboratories characterizing monoclonal antibodies (mAb) now have additional hydrophobic interaction chromatography (HIC) selectivity options, thanks to the expanded family of Thermo Scientific MAbPac HIC HPLC columns.
These hydrophobic groups could significantly enhance the association between these macromolecular chains and the organics in the wastewater through hydrophobic interaction.
Many laboratories analyzing monoclonal antibodies (mAb) regularly encounter situations where they need alternative hydrophobic interaction chromatography (HIC) selectivity.
18] reported that, on binding of butyl orange by bovine serum albumin, urea reduces the structure of the aqueous environment of the dye and the polycation to participate in the formation of hydrophobic interaction.
SynCo's and CBLI's development team's mixture of experience and intuition led them to recommend hydrophobic interaction chromatography as the next step after ion exchange, despite it usually being avoided if at all possible, due to its variable, and somewhat unpredictable performance.