This course discusses the principles of genetics with application to the study of biological function at the level of molecules, cells, and multicellular organisms, including humans. The topics include: structure and function of genes, chromosomes and genomes, biological variation resulting from recombination, mutation, and selection, population genetics, use of genetic methods to analyze protein function, gene regulation and inherited disease.Prepared by: Professor Chris Kaiser, Professor Gerry Fink and Professor Leona Samson
This course focuses on the mechanisms by which the amino acid sequence of polypeptide chains (proteins), determine their three-dimensional conformation. Topics in this course include sequence determinants of secondary structure, the folding of newly synthesized polypeptide chains within cells, folding intermediates aggregation and competing off-pathway reactions, and the unfolding and refolding of proteins in vitro. Additional topics covered are the role of helper proteins such as chaperonins and isomerases, protein recovery problems in the biotechnology industry, and diseases found associated with protein folding defects.
| Introduction to the problem | (PDF) |
| The Anfinsen experiments | (PDF) |
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Globular protein structure Protein interiors |
(PDF) |
| Using the Protein database (PDB) | (PDF - 2.5 MB) (Courtesy of Prof. David Gossard) |
| Helix-helix packing in globular proteins | (PDF) |
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Beta-sheets Beta-sheet packing |
(PDF) |
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Thermal denaturation Coiled coils Refolding of tropomyosin |
(PDF 1) (Courtesy of Prof. David Gossard) (PDF 2) |
| S-peptide helical folding | (PDF) |
| Detecting partially folded intermediates | (PDF) |
| Cytochrome c refolding pathway | (PDF) |
| Collagen structure and folding in vivo | (PDF - 1.8 MB) (Courtesy of Prof. David Gossard) |
| Protein misfolding and aggregation | (PDF) |
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Ribosome channel Nascent chains Trigger factor |
(PDF) |
| Chaperonin assisted folding | (PDF) |