title: Prediction of protein retention in hydrophobic interaction chromatography.
abstract: Hydrophobic interaction chromatography (HIC) is a powerful technique for protein separation. This review examines methodologies for predicting protein retention time in HIC involving elution with salt gradients. The methodologies discussed consider three-dimensional structure data of the protein and its surface hydrophobicity. Despite their limitations, the methods discussed are useful in designing purification processes for proteins and easing the tedious experimental work that is currently required for developing purification protocols.
authors.affiliation: Center for Molecular Studies of Cell, Institute for Biomedical Sciences, University of Chile, Independencia 1027, Santiago, Chile. amahn_2000@yahoo.es
authors.forename: Andrea
authors.initials: A
authors.lastname: Mahn
authors.forename: Juan A
authors.initials: JA
authors.lastname: Asenjo
mesh_terms: D000327:Adsorption; D001665:Binding Sites; D002845:Chromatography / Q000379:methods*; D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012997:Solvents / Q000737:chemistry*; D055672:Static Electricity; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D012997:Solvents; D014867:Water