Presented by: Ewa Folta-Stogniew, Ph.D., Director, Keck Biophysical Resource, Yale University School of Medicine
Presented Live: December 5, 2017
Static light scattering (SLS) is an analytical technique for determination of molar masses (molecular weights) and radii of gyration of macromolecules in solution. Measurement of molar mass from an SLS experiment determines the oligomeric state and thus provides association stoichiometry for biological macromolecules such as native and modified proteins and their complexes.
This webcast presents several case studies of the application of size exclusion chromatography (SEC) coupled with multi-angle (static) light scattering (MALS) in analysis of protein structure-function relationship, carried out at the Biophysics Resource of Keck Biotechnology Research Laboratory at Yale University School of Medicine.The examples include studies of heparin-induced dimerization of anaplastic lymphoma kinase (ALK), determination of stoichiometry of nucleic-acid repressor complex involved in regulation of transcription of the c-myc oncogene, deciphering the pathway of oligomerization and higher-order assembly of PopZ polar scaffold protein that supports asymmetric cell division, and re-examination of the role of amino-terminus in dimerization of SecA protein