title: Characterization of STAT self-association by analytical ultracentrifugation.
abstract: Multiple experimental tools have demonstrated that cytokine-induced STAT activation entails the transition of dimer conformations rather than de novo dimerization. In this chapter, we describe the utilization of analytical ultracentrifugation (AUC) as a powerful technique for the quantitative analysis of hydro- and thermodynamic properties of STAT proteins in solution. These studies provided a quantitative understanding of dimer stability and conformational transitions associated with the activation of STAT1.
authors.affiliation: School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK.
authors.forename: Nikola
authors.initials: N
authors.lastname: Wenta
authors.forename: Uwe
authors.initials: U
authors.lastname: Vinkemeier
mesh_terms: D057446:Hydrodynamics; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D050791:STAT Transcription Factors / Q000737:chemistry*; D012996:Solutions; D013816:Thermodynamics; D014461:Ultracentrifugation / Q000379:methods*
chemical_list: D050791:STAT Transcription Factors; D012996:Solutions