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Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
April 13 - 26, 2004
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. This course is supported with funds provided by the National Cancer Institute.
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Organized by:
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Richard Burgess, Albert Courey, Sue-Hwa Lin & Konstantin Severinov |
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Deadline for Abstracts:
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Application deadline: January 15, 2004
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Registration:
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Please apply here
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E-mail:
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meetings@cshl.edu
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