Can you help with a drawn step by step mec 2. Tryptophan in a peptide chain is a major target of singlet oxygen. Please provide twopossible products of the reaction of '02 with tryptophan and a mechanism for theirformation. Note that the benzene ring is unreactive.R-NHΙΖR102Two productsNHTryptophan in a peptide

Answered: 2. Tryptophan in a peptide chain is a…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 20P

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1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine protease
1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
The S3’ pocket on PfSUB1 (attached) contains the side chains of Lys465 and Tyr427. Researchers discovered that the Km for substrates with acidic residues in the P3’ position are much lower than those with nonpolar resides at the P3’ position in PfSUB1. Explain the Km data.
(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
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2
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
1
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
If you were to mutate Ser195 in the catalytic triad of chymotrypsin to another amino acid, which amino acid change would you expect to have the least effect on chymotrypsin catalytic activity? O Ala O Val O Phe O Thr O Leu
What would be the effect on the activity of phosphofructokinase of the mutation of Asp103 to the unusual amino acid shown below? Explain in terms of actual structures of the side chains of Asp and this unusual amino acid.

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2. Tryptophan in a peptide chain is a major target of singlet oxygen. Please provide two possible products of the reaction of '02 with tryptophan and a mechanism for their formation. Note that the benzene ring is unreactive. R -NH ΙΖ R 102 Two products N H Tryptophan in a peptide