Event Information
New Methods for the Thermodynamic Analysis of Protein Folding and Ligand Binding using Phosphorylase b as a Model System
- Abstract:
Several new experimental protocols were developed to make domain-specific thermodynamic stability measurements in large multi-domain and multi-subunit proteins. One protocol was based on a recently reported amide H/D exchange and mass spectrometry-based approach using the SUPREX technique in combination with protease digestion. Another protocol was based on a new chemical modification and mass spectrometry-based approach, termed SPROX, and a met-peptide enrichment protocol. Phosphorylase b (Phb) was used as a model multimeric protein system to validate and develop the above techniques. Our SUPREX with protease-digestion results generated three sets of thermodynamic parameters for what appear to be three distinct protein folding behaviors in Phb. Our results also provide the first demonstration of a new SPROX and met-peptide enrichment protocol.
Preliminary Examination Seminar
Student Exams Seminar