11 20 Sept 2010

11 20 Sept 2010 - LEHNINGER PRINCIPLES OF BIOCHEMISTRY Fifth Edition David L Nelson and Michael M Cox © 2008 W H Freeman and Company CHAPTER 5

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Unformatted text preview: LEHNINGER PRINCIPLES OF BIOCHEMISTRY Fifth Edition David L. Nelson and Michael M. Cox © 2008 W. H. Freeman and Company CHAPTER 5 Protein Function Nomenclature Ligand – molecule for which a protein has specific affinity Binding site – the area of a protein involved in the specific interaction with a ligand Lock-and-Key – model for specific recognition based on size, shape and complimentarity Induced fit – the structural change in a protein that occurs when ligand binds Enzyme – the subset of proteins which catalyze chemical reactions Substrate – the subset of ligands of which enzymes recognize Active site – the binding site of enzymes Use algebraic equations to analyze activity association Protein plus Ligand Protein-Ligand Complex dissociation P + L PL k a k d k a is the rate of association k d is the rate of dissociation K a = = [PL] [P][L] k a k d K d = = [PL] [P][L] k a k d K a = equilibrium association constant K d = equilibrium dissociation constant K d [P][L] [PL] = The K d equation solved for [PL] Total protein = [P] + [PL] Fraction of protein bound to ligand ( θ ) = [P] total [PL] Use the Kd expression of [PL] θ = [L] [L] + K d This assumes that [L] = [L] total θ is a hyberbolic function The K d is [L] at 50% bound protein What are the K d s for ligands X and Y? Carrier proteins have specific binding activity but do not...
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This note was uploaded on 09/18/2011 for the course CHEM 3510 taught by Professor Mueser during the Spring '10 term at Toledo.

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11 20 Sept 2010 - LEHNINGER PRINCIPLES OF BIOCHEMISTRY Fifth Edition David L Nelson and Michael M Cox © 2008 W H Freeman and Company CHAPTER 5

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