Biochemistry 2280A Lecture Notes - Lecture 4: Dissociation Constant, Equilibrium Constant, Fibril
9 Jun 2016
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Several hundred thousand in our bodies: protein topography. Proteins surfaces have a huge variety of shapes and charge distributions. Proteins undergo conformational changes (slight changes in shape) in response to minor changes in the environment or by the binding of some other molecule. Often involve changes in the relative positions of structural domains. Many proteins contain sites to which ligands specifically bind and form a complex with the protein. Kd (dissociation constant) is a measure of the strength or affinity of the interaction between the ligand and the protein, how much they attract each other. For a protein (p) binding ligand (l): Small kd = more complex than free molecules, high affinity. Large kd = more free molecules than complex, low affinity. A single unit made up of many units. Each protein much recognize and bind to others in the complex, thus assembling into a supramolecular structure.
