BCH 369 Lecture Notes - Lecture 8: Catalytic Triad, Chymotrypsin, Activation Energy
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2 use an enzyme to lovir activation energy. Enzyme catalyst most are protein some au rna. Chymotrypsin catalyzes the hydrolysis of peptide bonds catalytic triad. It also provides c theright place charge stabilizing so how does chymotrypsin speedup the eaction. By stabilizing the transition state energy reducing the activation. Oxyanion hole stabilize the transition state c is more. By fallingintothe whole the peptide susceptible to be broken. Why does this haeeen if sennepka is b and his is 6 g having thecharged amino acids dose together alters the pka of the middle amino group in det positive charges close together cause det to easily lose proton. What if adding a protein histedw in a. Solution no you need enzyme actuesile severe and environment. It only cleaves certain aas peptide e just anypeptide bond that follow bonds for. Pk tyr or trp in chymotrican"s substrate i yy euo no gene page. Are about 50 identical in aa sequence i.
