April 8 - 21, 2015
Application Deadline: March 2, 2015

Albert Courey,
University of California, Los Angeles
Sue-Hwa Lin, UT M.D.Anderson Cancer Center
James Love, Albert Einstein College of Medicine
Sergei Nechaev, University of North Dakota Sch of Medicine
Michael Marr, Brandeis University

See the roll of honor - who's taken the course in the past

This course is for scientists who are not familiar with techniques of protein isolation and characterization. The course is extremely rigorous and includes laboratory work during the days, as well as lectures with discussions and student talks in the evenings. Students are typically graduate students, postdoctoral scholars, staff scientists, and professors with specialized scientific expertise who now need to learn about protein purification and characterization. The course emphasizes laboratory strategies and current best practices in the field.

Each student in the course will become familiar with major techniques in protein purification by performing four separate isolations:

1) Regulatory protein (calmodulin) from muscle tissue (chicken gizzards),

 2) Sequence-specific DNA-binding protein (transcription factor AP1) from HeLa cell nuclei,

3) Recombinant protein overexpressed as inclusion bodies in E. coli, and

4) Membrane-bound protein (insulin receptor) from rat liver.

Students will be divided into groups and spend three days in each of the above four modules. In addition to the primary purification in a given module, a number of relevant characterizations will be performed on each protein, giving students experience with immunological and biochemical assays, peptide mapping, protein sequencing, and mass spectrometry. Students will learn bulk fractionation, electrophoretic, and chromatographic techniques, including: precipitation by salts, pH, and ionic polymers; ion exchange, gel filtration, hydrophobic interaction, and reverse phase chromatography; lectin affinity, ligand affinity, oligonucleotide affinity, and immunoaffinity chromatography; polyacrylamide gel electrophoresis and electroblotting; and, high performance liquid chromatography. Students will also learn procedures for solubilizing proteins from inclusion bodies and refolding them into active monomeric forms. Evenings in the course will involve lectures about topics that complement the laboratory curriculum: protein structure; modification of proteins; methodologies for protein purification, stabilization, and characterization; and, applications of protein biochemistry to molecular cell biology and cancer research.

This course is supported with funds provided by: National Cancer Institute

Cost (including tuition, board and lodging): $3,735

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are accepted into the course.