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Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory
April 15-28, 2009
This course is for scientists who are not familiar with techniques of protein isolation and characterization. It is a rigorous program that includes laboratory work all day and a lecture with discussion session every evening. Each student will become familiar with each of the major techniques in protein purification by actually performing four separate isolations including: (i) a regulatory protein from muscle tissue: (ii) a sequence-specific, DNA binding protein: (iii) a recombinant protein overexpressed in E. coli; and (iv) a membrane-bound receptor. A variety of bulk fractionation, electrophoretic, and chromatographic techniques will include: 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. Procedures will be present for solubilizing proteins from inclusion bodies and refolding them into active monomeric forms. Methods of protein characterization will be utilized to include immunological and biochemical assays, peptide mapping, amino acid analysis, protein sequencing, and mass spectrometry. Emphasis will be placed on strategies of protein purification and characterization. Guest lecturers will discuss protein structure, modification of proteins, methodologies for protein purification and characterization, and applications of protein biochemistry to cell and molecular biology.
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Organized by:
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Karen Adelman, NIEHS/National Institutes of Health; Richard Burgess, University of Wisconsin; Albert Courey, UCLA; Sue-Hwa Lin, University of Texas; Michael Marr, Brandeis University |
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Invited Speakers:
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To be announced
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Deadline for Abstracts:
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Application Deadline January 15
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Registration:
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Online Application Information
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E-mail:
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meetings@cshl.edu
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