A Review of Methods Used for Identifying Structural Changes in a Large Protein Complex
Identifieur interne : 000268 ( Ncbi/Curation ); précédent : 000267; suivant : 000269A Review of Methods Used for Identifying Structural Changes in a Large Protein Complex
Auteurs : Owen W. Nadeau ; Gerald M. CarlsonSource :
- Methods in molecular biology (Clifton, N.J.) [ 1064-3745 ] ; 2012.
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.
Url:
DOI: 10.1007/978-1-61779-334-9_7
PubMed: 22052488
PubMed Central: 3674763
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<front><div type="abstract" xml:lang="en"><p id="P1">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.</p>
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