drake7 - Protein Binding Phenomena Lecture 7, Medical...

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Unformatted text preview: Protein Binding Phenomena Lecture 7, Medical Biochemstry Ligands Ligand - any molecule that can bebound to a macromolecule (e.g., a protein). Examples of ligands include molecules ranging from small organic metabolites like glucose or ATP to large molecular polymers like glycogen or proteins. For our purposes, any molecule that can bind to a protein can be termed a ligand Why do ligands bind proteins? Both ligand and protein are surrounded by a water solvent shell. Each is undergoing random thermal motions that can lead to randomly oriented collisions between the protein and the ligand. Except for v. large ligands, thermally driven diffusion of the ligand is much more rapid than that of the protein. Ligand Binding (cont) Both protein and ligand can have functional groups such as hydroxyl, carboxyl, amino, amide and alkyl groups in various degrees of contact with the aqueous solvent. These functional groups on the ligand and on the protein may be capable of forming non- covalent bonds with each other. Ligand Binding (cont) If these functional groups are oriented during a collision so that they are spatially near one another, binding may occur. Of course, different ligands will have different spatial orientations of these functional groups and therefore will require different configurations of functional groups on the surface of the protein to permit binding. This matching of functional group spatial orientations are what determines the specificity of binding to that particular protein. Each protein will have its own characteristic set of binding specificities. Lock and Key Binding Model...
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drake7 - Protein Binding Phenomena Lecture 7, Medical...

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