Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys.
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- 3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys. Instructions Make use of the table below to determine the sequence of the mystery protein.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?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?
- VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.1. Gemtuzumab and Trastuzumab emtansine are two examples of mAb-drug conjugates (ADCS) where the thiol-containing drugs calicheamicin and DM1, respectively, are attached to the mAb's via the linkers shown below. SO, Na „SH Thiolhydrazide in Gemtuzumab Sulfo-SMCC in Trastuzumab emtansine (i) Show the chemistry involved in conjugating the drug (Calicheamicin-SH) to the antibody in Gemtuzumab and draw the target mAb-drug conjugate with a detailed linker region. Show the chemistry involved in conjugating the drug (DM1-SH) to the antibody in Trastuzumab and draw the target mAb-drug conjugate with a detailed linker (ii) region.1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
- 1. Amino acid analysis of the peptide gave the following residues: Asp Met The following facts were observed: a) Trypsin treatment had no effect. b) The phenylthiohydantoin released by Edman degradation was Leu Lys Phe Tyr What is the amino acid sequence for this heptapeptide? H C-C-CH₂ H c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. d) Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys.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: a) Trypsin treatment had no effect. b) The phenylthiohydantoin released by Edman degradation was -C-CH₂ What is the amino acid sequence for this heptapeptide? OH c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. d) 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.a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
- 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 protease3. Subtilisin (Mol. weight 27,600) is a protease that can catalyze hydrolysis of certain amino acid esters and amides. For the synthetic substrate N-acetyl-L-tyrosine ethyl ester (Ac-Try-OEt), subtilisn exhibits Km and kcat values of 0.15 M and 550 s-¹, respectively. a) What is the Vmax when the subtilisin concentration is 0.4 mg/ml? b) Indole is a competitive inhibitor of subtilisin with a Ki of 0.05 M. What is the Vmax for Ac-Try-OEt hydrolysis by 0.4 mg/ml subtilisin in the presence of 6.25 mM indole? c) What is the Vo when 0.4 mg/ml subtilisin is incubated with 0.25 M Ac-Try-OEt and 1.0 M indole?1. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: - Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val - Molecular weight of the peptide was estimated to be aroung 1,200 Da - The peptide failed to undergo hydrolysis when treated with carboxypeptidase - Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val- - Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain By using the above information, deduce the amino acid sequence of this peptide antibiotic. Write the final peptide sequence using 3-letter abbreviations. Show the complete and step by step solution.