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MBB222-lecture9 - Protein Function General Strategies for...

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Protein Function General Strategies for Enzyme Action
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only a few residues in the active site participate in catalysis - these are typically residues that are distant in the primary sequence but come together in the 3D folded structure of the protein.
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the active site residues typically form multiple, weak, noncovalent interactions with the substrate these combined interactions are highly specific and short- i i l l l i b h range, requiring molecular complementarity between the substrate and the active site the full complement of these interactions is formed only the full complement of these interactions is formed only during the transition state
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the bonds between the enzyme and the transition state substrate adds state substrate adds stability and thus lowers the activation energy ‘ES’ and ‘EP’ represent lower energy intermediates in the intermediates in the reaction pathway
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Enzyme Kinetics: study of the rates of chemical reactions if we graph reaction velocity vs. substrate concentration for varying substrate concentration for varying amounts of substrate and a fixed amount of enzyme results in hyperbolic curve initial slopes are very steep, but then begin to plateau then begin to plateau, approaching a maximal value reaction velocity refers to the change in substrate concentration with respect to time
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