title: A review of methods used for identifying structural changes in a large protein complex.
abstract: This chapter explores the structural responses of a massive, hetero-oligomeric protein complex to a single allosteric activator as probed by a wide range of chemical, biochemical, and biophysical approaches. Some of the approaches used are amenable only to large protein targets, whereas others push the limits of their utility. Some of the techniques focus on individual subunits, or portions thereof, while others examine the complex as a whole. Despite the absence of crystallographic data for the complex, the diverse techniques identify and implicate a small region of its catalytic subunit as the master allosteric activation switch for the entire complex.
authors: Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
authors: Owen W
authors: OW
authors: Nadeau
authors: Gerald M
authors: GM
authors: Carlson
mesh_terms: D000494:Allosteric Regulation / Q000502:physiology; D002118:Calcium / Q000494:pharmacology; D031541:Fluorescence Resonance Energy Transfer; D007120:Immunochemistry; D008854:Microscopy, Electron; D011487:Protein Conformation / Q000187:drug effects; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D011506:Proteins; D002118:Calcium