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The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. [19] The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. [3]
[7] [9] Hydrophobic molecules can be eluted from the column by decreasing the polarity of the mobile phase using an organic (non-polar) solvent, which reduces hydrophobic interactions. The more hydrophobic the molecule, the more strongly it will bind to the stationary phase, and the higher the concentration of organic solvent that will be ...
The driving mechanism for micellization is the transfer of hydrocarbon chains from water into the oil-like interior. This entropic effect is called the hydrophobic effect. Compared to the increase of entropy of the surrounding water molecules, this hydrophobic interaction is relatively small. The water molecules are highly ordered around the ...
The Hofmeister series or lyotropic series is a classification of ions in order of their lyotrophic properties, which is the ability to salt out or salt in proteins. [ 1 ] [ 2 ] The effects of these changes were first worked out by Franz Hofmeister , who studied the effects of cations and anions on the solubility of proteins .
Water on hydrophobic surfaces will exhibit a high contact angle. Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. [2]
The four fundamental classes of forces and interaction in protein adsorption are: 1) ionic or electrostatic interaction, 2) hydrogen bonding, 3) hydrophobic interaction (largely entropically driven), and 4) interactions of charge-transfer or particle electron donor/acceptor type. [7]
Examples include, partial molar heat capacity, transition temperature and surface tension. Physical methods are easy to use and flexible in terms of solute. The most popular hydrophobicity scale was developed by measuring surface tension values for the naturally occurring 20 amino acids in NaCl solution. [ 30 ]
In pure water, the interactions between the resin and the hydrophobic regions of protein would be very weak, but this interaction is enhanced by applying a protein sample to HIC resin in a high ionic strength buffer. The ionic strength of the buffer is then reduced to elute proteins in order of decreasing hydrophobicity. [9]