title: Detecting protein-protein interactions by gel filtration chromatography.
abstract: Upon protein-protein interaction, the formed complex is subject to a change in size. A number of methods can be utilized to detect such a change. Gel filtration technology is well recognized for its ability to monitor and separate protein species of different sizes, and can greatly facilitate functional studies of protein complexes. In addition, gel filtration can be performed in any buffer system that preserves the protein complex formation and function. Therefore, it can be a significantly useful method for studying protein interactions. In this chapter, a protocol for performing gel filtration is described in detail.
authors: Department of Pharmacology, Emory University School of Medicine, 1510 Clifton Rd, Atlanta, GA, 30322, USA, yan.bai@emory.edu.
authors: Yan
authors: Y
authors: Bai
mesh_terms: D002850:Chromatography, Gel / Q000379:methods*; D007700:Kinetics; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D060066:Protein Interaction Maps; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins