![]() at 50% binding Saturation: there is a finite number of binding sites Competition: structurally similar molecules can compete for binding and remember: the protein can be an enzyme, receptor, transporter, etc. Protein-ligand binding properties Specificity: binding depends on ligand size, shape, charge Affinity: strength of binding: i.e. at 50% binding fig 3-31Īffinity (different ligands) strength of binding: i.e. at 50% binding fig 3-30Īffinity (different proteins) strength of binding: i.e. at 50% binding fig 3-29Īffinity & saturation strength of binding: i.e. Specificity protein Y specificity greater than protein X specificity fig 3-28Īffinity strength of binding: i.e. Specificity binding depends on ligand size, shape, charge fig 3-27 fig 3-26 at 50% binding Saturation: there is a finite number of binding sites Competition: structurally similar molecules can compete for binding Protein ligand interaction Proteins could be: Ligands would be: enzymes substrates, allosteric regulators receptors chemical messengers transporters transported substances transcription factors transcription regulators any of above drugs Gap junctions cell-cell communication, small molecules (<1000 MWt) cardiac intercalated disks, smooth muscle fig 3-10d kidney, gut) paracellular pathway between cells fig 3-10b Tight junctions cell “collar”, block large molecules, no lateral protein movement epithelial tissue (esp. Intercellular structures Desmosomes “spot welds”, dense proteins (cytoplasm & intercellular) fibers (intermediate filaments) extend across cells epithelial cells (especially skin), cardiac intercalated disks Tight junctions cell “collar”, block large molecules, no lateral protein movement epithelial cells Gap junctions cell-cell communication, small molecules (<1000 MWt) cardiac intercalated disks, smooth muscleĭesmosomes “spot welds”, dense proteins (cytoplasm & intercellular) fibers (intermediate filaments) extend across cells epithelial cells (especially skin), cardiac intercalated disks fig 3-10a Phospholipid structure Amphipathic molecule (phosphatidyl choline) hydrophobic part: fatty acids hydrophilic part: phosphate & choline ![]()
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