Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET

• DOI: 10.1073/pnas.1700357114
• Publication Date: 2017-08-01T00:50:22Z
• Authors: Hoi Sung Chung; Fanjie Meng; Jae-Yeol Kim; Kevin McHale; Irina V. Gopich; John M. Louis
• Keywords: Tetramer; Single-molecule FRET; Acceptor

Significance Intrinsically disordered proteins often form pathological oligomers implicated in various diseases. In many cases, these cannot be separated and characterizations of their sizes conformations are difficult. We develop a single-molecule fluorescence method that can probe individual without separation determine the equilibrium constants oligomerization kinetics. By combining two- three-color FRET spectroscopy with lifetime analysis, it is possible to flexibility unambiguously. apply this tetramerization domain p53 compare monomer, dimer, tetramer. This will useful exploring other protein systems involved important biological disease processes.