content · content 1. protein structure and function 2. exploring proteins 3. dna, rna & flow...
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Chimie biologique Physique 4ème sem 2006
CONTENT
1. PROTEIN STRUCTURE AND FUNCTION
2. EXPLORING PROTEINS
3. DNA, RNA & FLOW OF GENETIC INFORMATION
4. EXPLORING GENES
5. ENZYMES : BASIC CONCEPTS AND KINETICS
6. PORTRAIT OF AN ALLOSTERIC PROTEIN ch 10
7. MEMBRANE STRUCTURE AND DYNAMICS
8. MEMBRANE CHANNELS AND PUMPS
9. SIGNAL TRANSDUCTION
10. MOLECULAR MACHINES & PROTEIN DESIGN
11. ANTIBODIES AND T-CELL RECEPTORS
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Portrait of an allosteric protein: Hemoglobin
chapter 10, Stryer
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Allosteric enzymes
Do not obey Michaelis-Menten kinetics
Contain multiple subunits & multiple
active sites
Binding of substrate to one active site
affects properties of other active sites in
same enzyme molecule
Cooperativity: Binding of substrate to
one active site facilitates binding to others
Regulation of metabolic pathways:
Activity of allosteric enzymes are
adjusted for needs of cell
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3D structure of myoglobinKendrew 1957
Scheme of helices &
heme group
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Distribution of amino acids in myoglobin
Hydrophobic (yellow) Charged (blue) Others (white)
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Details of oxygen binding site in myoglobin
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!2"2 tetramer of human hemoglobinPerutz 1959 (started 1936)
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Hemoglobin transports oxygen efficiently by cooperative binding
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Oxygen binding markedly changes the quaternary structure
of hemoglobin
O2
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Position of iron in deoxyhemoglobin
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Oxygen binding induces structural changes
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Conformational changes in hemoglobin induced by oxygen binding
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Hemoglobin transports oxygen efficiently by cooperative binding