Related Experiment Video
Updated: Aug 2, 2026

Automated Hydrophobic Interaction Chromatography Column Selection for Use in Protein Purification
Published on: September 21, 2011
Prediction of protein retention in hydrophobic interaction chromatography
1Center for Molecular Studies of Cell, Institute for Biomedical Sciences, University of Chile, Independencia 1027, Santiago, Chile. amahn_2000@yahoo.es
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.
More Related Videos
Related Concept Videos
Protein-protein Interfaces
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Silica Gel Column Chromatography: Overview
Polar components tend to bind strongly to the silica gel, causing them to move slowly through the column. In contrast, nonpolar compounds...
High-Performance Liquid Chromatography: Introduction
In HPLC, two phases play a critical role in the separation process:
Size-Exclusion Chromatography
Silica particles offer advantages such as rigidity,...

