Historical Landmarks in Our Understanding of Proteins
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Transcript of Historical Landmarks in Our Understanding of Proteins
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Historical Landmarks in Our Understanding of Proteins• 1838 The name "protein" (from the Greek proteios, "primary") was suggested by Berzelius
for the complex organic nitrogen-rich substance found in the cells of all animals and plants.• 1819-1904 Most of the 20 common amino acids found in proteins were discovered.• 1864 Hoppe-Seyler crystallized, and named, the protein hemoglobin.• 1894 Fischer proposed a lock-and-key analogy for enzyme-substrate interactions.• 1897 Buchner and Buchner showed that cell-free extracts of yeast can ferment sucrose to form
carbon dioxide and ethanol, thereby laying the foundations of enzymology.• 1926 Svedberg developed the first analytical ultracentrifuge and used it to estimate the correct
molecular weight of hemoglobin.• 1933 Tiselius introduced electrophoresis for separating proteins in solution.• 1942 Martin and Synge developed chromatography, a technique now widely used to separate
proteins.• 1951 Pauling and Corey proposed the structure of a helical conformation of a chain of L-
amino acids -- the alpha helix -- and the structure of the beta sheet, both of which were later found in many proteins.
• 1955 Sanger completed the analysis of the amino acid sequence of insulin, the first protein to have its amino acid sequence determined.
• 1956 Ingram produced the first protein fingerprints, showing that the difference between sickle- cell hemoglobin and normal hemoglobin is due to a change in a single amino acid.
• 1963 Monod, Jacob, and Changeux recognized that many enzymes are regulated through allosteric changes in their conformation.
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Number & Size Distribution of Cellular Proteins
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Size & Shape Comparisons of Proteins
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Protein Structure and Function• Protein Structure
– Primary structure - amino acid sequence.
– Secondary structure - formation of helices and sheets.
– Tertiary structure - the three-dimensional conformation of a polypeptide chain.
– Quaternary structure - formation of a protein molecule as a complex of more than one
polypeptide chain.
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Protein Structure and Function• Protein Function
– Enzymes - proteases, synthetases, polymerases, kinases– Structural - extracellular collagen, elastin
intracellular tubulin, actin, -keratin– Transport - serum albumin, hemoglobin, transferrin– Motor - myosin, kinesin, dynein– Storage - ferritin, ovalbumin, calmodulin– Signaling - insulin, nerve growth factor, integrins– Receptor - acetylcholine receptor, insulin receptor, EGF
receptor– Gene regulatory - lactose repressor, homeodomain proteins– Special purpose - green fluorescent protein, glue proteins
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Protein Structure and Function• Protein Structure
– Primary structure - amino acid sequence.
– Secondary structure - formation of helices and sheets.
– Tertiary structure - the three-dimensional conformation of a polypeptide chain.
– Quaternary structure - formation of a protein molecule as a complex of more than one
polypeptide chain.
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Amino Acids
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Codon Usage Table
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Protein Folding
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Protein Denaturation & Refolding
Protein confirmation is determined solely by its amino acid sequence
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Protein Structure and Function• Protein Structure
– Primary structure - amino acid sequence.
– Secondary structure - formation of helices and sheets.
– Tertiary structure - the three-dimensional conformation of a polypeptide chain.
– Quaternary structure - formation of a protein molecule as a complex of more than one
polypeptide chain.
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helix Secondary Structure
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sheet Secondary Structure
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Noncovalent Bonds
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Noncovalent Bonds
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Hydrogen Bonds in Proteins
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Noncovalent Bonds
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Noncovalent Bonds
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Noncovalent Bonds
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Noncovalent Bonds
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sheet Secondary Structure
Antiparallel sheet
Parallel sheet
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helix Interactions with Phospholipids
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Protein Structure and Function• Protein Structure
– Primary structure - amino acid sequence.
– Secondary structure - formation of helices and sheets.
– Tertiary structure - the three-dimensional conformation of a polypeptide chain.
– Quaternary structure - formation of a protein molecule as a complex of more than one
polypeptide chain.
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Tertiary Structure
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Tertiary Structure
Cytochrome b Lactate dehydrogenase IgG light chain
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Structural Importance in Protein Function
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Coiled-coiled Structure of Multiple helices
• A single helix with amino acids a and d being nonpolar.
• B two helices wrap around each other with one nonpolar side
chain interacting with the nonpolar side chain of the other. The hydrophilic side chains are exposed to the aqueous environment.
• C atomic structure of a coiled-coil showing the nonpolar interactions in red
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Protein Structure and Function• Protein Structure
– Primary structure - amino acid sequence.
– Secondary structure - formation of helices and sheets.
– Tertiary structure - the three-dimensional conformation of a polypeptide chain.
– Quaternary structure - formation of a protein molecule as a complex of more than one
polypeptide chain.
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Quaternary Structure
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Quaternary Structure
Hemoglobin
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Protein - Protein Interactions
• A protein with just one binding site can form a dimer with an identical protein.
• Identical proteins with two different binding sites can form a long helical filament.
• If the two binding sites are located appropriately to each other, the protein subunits can form a closed ring instead of a helix.
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Collagen and Elastin
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Disulfide bonds