BIOC 2580 Lecture 2: Protein Functions.docx

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Examples of protein functions : protein flexibility is critical in order for it to undergo conformational changes (example in enzymes: enzyme: catalyzes covalent bond breakage or formation. E. g: protein kinase: structural: mechanical support to cells and tissues. E. g: hemoglobin: motor: generates movement in cells and tissues. E. g: myosin: storage: stores small molecules and ions. E. g: ferritin: signal: carries signals from cell to cell. E. g: insulin: receptor: detects signal and transmits them to the cell. E. g: rhodopsin: gene regulator: binds to dna to switch genes on or off. Sites where ligands can specifically bind and form a complex with the protein: ligand (molecule) fits perfectly at site, non covalent bonding (weak bonding) causing extreme specificity. Dissociation constant: kd is a measure of the strength/affinity of interactions (mols/l). P + l pl where p=ligand binding protein, l=ligand and pl=complex: kd= [p][l] Examples: calmodulin/calcium: 10^-6 m antibody/antigen: 10^-12 m estrogen/estrogen receptor biotin-streptavidin: 1. 0 fm=10^-15 m (very high affinity/tight binding)

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