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SC2: Buffer Optimization for Purifying Proteins

Sunday, January 20, 2013

5:00 - 8:00pm


This short course will review (i) common causes of protein aggregation during expression and purification, (ii) methods to detect the presence of aggregates, (iii) the types and properties of chemicals that, when added to buffers, may improve protein solubility, and (iv) finally methods to screen these additives to rapidly optimize the solubility of your protein.

5:00 Mario Lebendiker, Ph.D., Head, Protein Purification Facility, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem 

6:30 Dinner Break

7:00 Sarah E. Bondos, Ph.D., Assistant Professor, Molecular and Cellular Medicine, Texas A&M Health Science Center

8:00 Close of Short Course

 

SPEAKER Biographies: 

Mario Lebendiker, Ph.D., Head, Protein Purification Facility, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem

Mario LebendikerDr. Mario Lebendiker is in charge of the Protein Purification Facilities at the Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem. He is actively involved in many collaborations for structural and biochemical studies within the Hebrew University, others Universities in Israel, as well as with biotech and pharmaceutical companies. Dr. Lebendiker received a PhD in Biochemistry in 1982 from the Animal Virology Center (CEVAN), in Buenos Aires University, Argentina. Together with many other laboratories, he found the Protein Production and Purification Partnership in Europe (P4EU) network; a platform for the exchange of information, know-how and materials between core facility labs in the field of protein expression and purification.

Sarah E. Bondos, Ph.D., Assistant Professor, Molecular and Cellular Medicine, Texas A&M Health Science Center

Sarah BondosDr. Bondos studies protein folding, context-specific protein regulation, and protein aggregation and assembly. Her laboratory has discovered that long-range interactions between structured and intrinsically disordered regions within the Drosophila Hox transcription factor Ultrabithorax (Ubx) regulate DNA binding and transcription regulation in a tissue-specific manner. In vivo Ubx engages in many protein interactions, including homo-multimerization, and its monomers are extremely aggregation-prone in vitro. This property led the Bondos lab to develop methods to screen buffers for improved solubility in vitro to enable biophysical and developmental biological studies on Ubx regulation. The Bondos lab has also used these approaches to identify conditions that permit the controlled assembly of Ubx into ordered, elastic biomaterials.