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Hydrophobic interaction chromatography

O'Connor, Brendan and Cummins, Phil (2011) Hydrophobic interaction chromatography. In: Walls, Dermot and Loughran, Sinéad T., (eds.) Protein Chromatography. Methods in Molecular Biology, 681 . Humana Publishers Ltd., pp. 431-439.

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Most proteins and large polypeptides have hydrophobic regions at their surface. These hydrophobic ‘patches’ are due to the presence of the side chains of hydrophobic or non-polar amino acids such as phenylalanine, tryptophan, alanine and methionine. These surface hydrophobic regions are interspersed between more hydrophilic or polar regions and the number, size and distribution of them is a specific characteristic of each protein. Hydrophobic Interaction Chromatography (HIC) is a commonly used technique that exploits these hydrophobic features of proteins as a basis for their separation even in complex biological mixtures (1) (2). In general the conditions under which hydrophobic interaction chromatography is used are relatively mild and ‘protein friendly’ resulting in good biological recoveries. Hydrophobic binding is relatively strong and is maintained even in the presence of chaotrophic agents, organic solvents and detergents. For these reasons this technique has a widespread use for the purification of proteins and large polypeptides.

Item Type:Book Section
Uncontrolled Keywords:proteins; polypeptides
Subjects:Biological Sciences > Biotechnology
Biological Sciences > Biochemistry
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > Irish Separation Science Cluster (ISSC)
Publisher:Humana Publishers Ltd.
Official URL:
Copyright Information:© 2011 Springer (Humana) The original publication is available at
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
Funders:Science Foundation Ireland, Enterprise Ireland
ID Code:17810
Deposited On:28 Feb 2013 14:33 by Brendan O'Connor. Last Modified 02 Nov 2016 14:03

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