Can you help me with the mec 2. Tryptophan in a peptide chain is a major target of singlet oxygen. Please provide twopossible products of the reaction of 102 with tryptophan and a mechanism for theirformation. Note that the benzene ring is unreactive.R-NHNHZIR102Two productsTryptophan in a peptide

MECHANISMInitial Attack by Singlet Oxygen:Singlet oxygen (1O2) is an electrophilic species, that…

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. 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?
2. Amino acid analysis of the a heptapeptide gave the following residues: Asp Glu Leu Lys Met Tyr Trp NH4+. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was OH H C-C-CH₂ H. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a tetrapeptide that had a net positive charge at pH 7 and tripeptide that had a zero net charge at pH 7. What is the amino acid sequence for this heptapeptide?
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).
1
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.
о 6. What is the catalytic triad and what particular protein family would you find this? What is the general role of the catalytic triad? Predict what would happen if Asp were mutated to Gly. ructure formation of alpha heli
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2
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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.
Can you help with a drawn step by step mec
1. Draw all the forms of Tyrosine at pH 10.5. I have the predominant form and the protonation and deprotonation values written out, but I'm not sure how to draw the other forms now. 2. Draw the peptide chain arginyl-alanyl-histidyl-cysteinyl-isoleucyl-asparagine at pH 7

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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 102 with tryptophan and a mechanism for their formation. Note that the benzene ring is unreactive. R -NH N H ZI R 102 Two products Tryptophan in a peptide