Biophysics Seminar - 10/10/2007 - 2:30pm - 170 DHLRI

Membrane Insertion of the Bacillus thuringiensis Cry1Ab Toxin: Single Mutation in Domain II Blocks Partitioning
Manoj Nair

Mapping functional epitopes in the human prolactin hormone
Geeta Vittal-Rao

Human prolactin activates the human prolactin receptor by binding the extracellular domains of two prolactin receptors. This project deals with identifying the contribution of individual amino acid residues in human prolactin that are involved in binding prolactin receptor. In other words, the goal of this project is to identify the functional epitopes in the human prolactin hormone. To this end, I have made 104 Alanine mutants of human prolactin. We have reason to believe that these 104 amino acids account for 80-90% of the free energy of binding of human prolactin to its receptor. We have over expressed these 104 mutants and have purified them by ion-exchange chromatography. We are currently working on obtaining an appropriate ligand for performing tripartite binding studies that would use hormone and secondary receptor as analytes in the SPR experiment.

Last update: 10/09/2007, Ralf Bundschuh