Lecture 27

Lecture 27 - Lecture 27 Regulation of Protein Function...

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Lecture 27 Regulation of Protein Function Regulation by changes in conformation: Allostery + cooperativity Common regulators: Calcium GTP Phosphorylation/dephosphorylation Allostery Definition : Binding of one ligand influences binding of another ligand in a different region of the protein Property of changing the structure of a protein Influences the binding of something else Ligand interactions always influences protein conformation to a certain extent: Need to determine effect and magnitude of the interaction When two molecules interact they change Positive allostery Positive allostery: Binding of A favour binding of B A : Can be a molecule, salt or nucleotide, lipid that binds Binding induces a change in conformation in the structure of the protein Propagates through the protein Charges the binding site for another protein Negative allostery Page | 1
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Negative allostery : Binding of A disfavours binding of B A comes in, propagates and changes the conformation of a binding site B has to leave Change in structure: No dramatic changes Little tweeking of the structure that exposes a few residues at the surface of the pocket Cooperativity Definition : Binding of A to blue protein doesn't only influence B but could influence the binding of another ligand of the same kind In most cases its rare to have two identical binding sites for the same ligand on the same polypeptide: Nature works by copies
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This note was uploaded on 06/05/2011 for the course BIO 200 taught by Professor Thomasebureau during the Fall '07 term at McGill.

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Lecture 27 - Lecture 27 Regulation of Protein Function...

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