Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10231693 | Biotechnology Advances | 2005 | 10 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Andrea Mahn, Juan A. Asenjo,