lecture0224final - Resolving enzyme mechanisms Many enzymes...

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Resolving enzyme mechanisms Many enzymes can be crystalized Since 40-60% of the mass of a  protein crystal is solvent -   substrates may have access to the  active site -   if the protein has folded  in the crystal correctly into its native  state    And the enzyme may be active -  small structural changes needed  during the reaction may be possible.
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Resolving enzyme mechanisms Substrate molecules can be  synchronously released inside the  enzyme crystal from “photochemical  cages” – molecules that inactivate or  surround the substrate, but release it  upon a pulse of light from a laser. After the release, ultra-high intensity X- ray crystallography can take “snapshots”  of the structure of the enzyme and  substrate as the reaction proceeds. The enzyme-substrate complex and reaction  intermediates can also be stabilized by  sudden cooling Site directed mutations of the enzyme can be  developed to test the involvement of specific  R-groups  or to “trap” the reaction at a  specific stage
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The most basic model of enzyme  kinetics – the Michaelis-Menten  equation, relates the:
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lecture0224final - Resolving enzyme mechanisms Many enzymes...

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