A mutant form of polypeptide hormone angiotensin II has the amino acidcomposition(Asp, Arg, Ile, Met, Phe, Pro, Tyr, Val)The following observations are made:Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptidewith all the rest.• Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro,and a hexapeptide containing all the others.• Chymotrypsin cleaves the hormone into two tetrapeptides, ofcomposition(Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro)• The dipeptide of composition (Pro, Phe) cannot be cleaved by eitherchymotrypsin or carboxypeptidase.What is the sequence of angiotensin II?

Introduction: The amino acids are combined by an amide or peptide bonds. The series of amino acids…

Answered: A mutant form of polypeptide hormone…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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A mutant form of polypeptide hormone angiotensin II has the amino acidcomposition (Asp, Arg, Ile, Met, Phe, Pro, Tyr, Val)The following observations are made:• Trypsin yields a dipeptide containing Asp and Arg and a hexapeptide withall the rest.• Cyanogen bromide cleavage yields a dipeptide containing Phe and Proand a hexapeptide containing all the others.• Chymotrypsin cleaves the hormone into two tetrapeptides, of composition (Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro)• The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase.What is the sequence of angiotensin II?
A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr. Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase. What is the amino acid sequence of this polypeptide?
A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr, Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) What is the amino acid sequence of this polypeptide?
Show where trypsin and chymotrypsin would cleave the following peptide. Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-GlnB. After treatment with peroxyformic acid, the peptide hormone vasopressin is partially hydrolyzed. The following fragments are recovered. Propose a primary structure for vasopressin.Phe-Gln-Asn Pro-Arg-Gly • NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gln-AsnC. Consider the following peptide: Gly-Ile-Glu-Trp-Thr-Pro-Tyr-Gln-Phe-Arg-LysWhat amino acids and peptides are produced when the above peptide is treated with each of the following reagents?1. Carboxypeptidase2. Chymotrypsin3. Trypsin 4. DNFBD. From the analytical results, deduce the primary structure of a peptide isolated from the Atlantian orchid that contains 14 amino acids.Complete hydrolysis produces the following amino acids: Gly (3), Leu (3), Glu (2), Pro, Met, Lys (2), Thr, Phe. Treatment with carboxypeptidase releases glycine. Treatment with DNFB releases DNP- glycine. Treatment with a…
TPCK and TLCK are irreversible inhibitors of serine proteases. One ofthese inhibits trypsin and the other chymotrypsin. Which is which? Explainyour reasoning. Suggest the effects of each of the following mutations on the physiologicalrole of chymotrypsinogen:(a) R15S(b) C1S(c) T147S
Neuraminidase (NA) catalyzes a hydrolysis of the glycosidic linkages of sialic acids using a mechanism shown in Fig. (a). and Fig. (b) shows competitive inhibitors of NA Considering the mechanism of NA, why do zanamivir and oseltamivir inhibit NA so potently?
Snake venom contains many hydrolase enzymes, including several serine proteases. One such protease (present in high concentrations in snake venom) mimics the action of thrombin to activate fibrin. The venom protease cleaves peptide bonds with a specificity for basic, positively charged amino acids. This enzyme is incubated with a substrate peptide with the sequence SNPDCKVALYMTW. Draw a mechanism for the peptide hydrolysis of this specific peptide catalyzed by this snake venom protease. Include the structure of the active site amino acids of the enzyme and the substrate peptide group (including the full structure of the 2 specific amino acids that contribute to the scissile peptide group in the substrate) in your mechanism. Use the curved arrow convention to illustrate the flow of electrons.
Insulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?
One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below 1) Provide a brief explanation as to why ligand binding toproteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.
The protein fragments ABS1 and ABS2 of tropomodulin were produced as fusion proteins with chitin binding domain and purified by a chitin column. Explain the principles of this type of affinity chromatography and support it with a self‐drawn figure. This is with regards to Tropomodulin/ F-Actin complex.
A study is conducted to assess the molecular mechanisms of hormone X. A radioactively labeled form of this hormone is incubated with human cells in tissue culture for 30 minutes, and then incubated briefly with a cross-linking agent. The plasma membrane, cytosolic, and nuclear fractions are isolated from the cell lysate, and the subcellular proteins are separated from these fractions by gel electrophoresis. The only protein bound to the labeled hormone is identified in the new clear fraction. Hormone X is most likely which of the following? Epinephrine Glucagon Growth hormone Insulin Thyroxine
Which of the following regulatory mechanisms will specifically inhibit pyrimidine synthesis (and not also purine synthesis)? (A) allosteric regulation of aspartate transcarbamoylase by CTP(B) allosteric regulation of aspartate transcarbamoylase by ATP(C) synergistic inhibition of PRPP synthetase by AMP/GMP/IMP(D) synergistic inhibition of PRPP amidotransferase by AMP/GMP/IMP (E) feedback inhibition of ribonucleotide reductase by dATP

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