Please answer in full explaination 2.2 Complete hydrolysis of a hexapeptide by 6M HCI at 110°C followed byamino acid analysis indicated the presence of Cys, Met and Gly in anequal ratio. Complete digestion of the peptide with cyanogen bromideafter a denaturation step with ß-mercaptoethanol yielded two smallerpeptides of the same molecular weight.A) Identify amino acids in the scheme below and write their names intoprovided boxes:B) Name the N-terminal and C-terminal amino acids of this peptide:N-terminal:SISC-terminal:

The hydrolysis of the given peptide gives an equal ratio of cysteine, methionine, and glycine. It…

Answered: 2.2 Complete hydrolysis of a…

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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describe a detailed experimental procedure for the chemical synthesis of proteins with the α-ketoacid hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.
2. 4. The sequence of a peptide A formed by 16 amino acids was determined using a combination of methods that included the use of the Sanger's reagent, protease treatment and SDSPAGE/2D-electropheresis. The following data was obtained from the mentioned experiments: (a) Treatment of peptide A with an excess of fluoro-2,4-dinitrobenzene followed by peptide digestion with concentrated HI and analysis of the hydrolysate showed the presence of 2,4-dinitroderivatives of Ala and Glu. (b)Treatment of the same peptide with carboxypeptidase A resulted in free Tyr and free Ala. (c) SDS-PAGE of peptide A showed only one band at a molar mass of 18 kDa. After treatment with ß-mercaptoethanol and a second electrophoresis trial, one band appeared on the gel but this time the molar mass of the band was approximately 900 Da. Isoelectric focusing of the peptide isolated from this band resulted in two separate bands at pl 9.8 and 4.5 (d) After treatment of peptide A with beta-mercaptoethanol and…
A certain plant storage protein, after being isolated, was digested using both 8N H2SO4 and conc. Ba(OH)2. The resulting hydrolysates were then analyzed for amino acid composition using paper chromatography with EtOH-NH3-H2O (80:10:10) as the solvent system and ninhydrin as the visualizing agent. Name the amino acids found in the acid hydrolysate labelled 1-5.
One sample of the globular protein peroxidase is hydrolyzed by heating with 6 M HC1. A second sample is denatured by treatment with acetone. a) How does the peroxidase structure change during hydrolysis? Will this change the biological activity of peroxidase? b) How does the peroxidase structure change during denatur-ation? Will this change the biological activity of perox-idase? c) Are either of these processes likely to be reversible?
Draw the linear fisher projections of D-ribarnic acid, L-xyluronic acid, D-arabinuronic acid, L-gluconate, D-mannarate, L-idarate and D-galacturonate, and D-lyxonate
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
Determine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.
22) A) Write the structure for a generic triacvlglyceride at pH 7.4. B) Show the mechanism of a lipase including the catalytic triad and the oxyanion hole up to the tetrahedral intermediate of the cleavage of the acyl-alcohol bond. C) What is the purpose of the þxyanion hole? D) How does the catalytic triad function to lower the pKa of serine. coo coo H,N-C-H H,N-C-H CH, CH2 он Serine (S) (Ser) HN Histidine (H) (His) coo co H,N-C-H H,N-C-H H CH, Glycine (G) (Gly) coo Aspartate [D] (Asp)
Draw structural formulas for the products obtained when the tripeptide Thr-Leu-Ile undergoes complete hydrolysis under acidic conditions
Amino acid analysis of a decapeptide gave the following residues: Ala (2), Gly, Leu, Lys (2), Met, Phe, Trp, Val Subjecting the decapeptide to various chemical/ enzymatic hydrolysis yields the following fragments: Cyanogen bromide: Leu-Ala-Met and a heptapeptide Trypsin: Phe-Ala-Lys and a heptapeptide Chymotrypsin: Gly-Val-Lys-Phe, Ala-Lys, Leu, and a tripeptide • Thermolysin: Phe-Ala-Lys, Leu-Ala-Met, and two dipeptides . Note that the intact decapeptide was used in each treatment. 1. What is the sequence of the heptapeptide produced upon treatment with trypsin? Fill each blank with the three-letter designation of the amino acid residue from the N-terminus to the C-terminus. 2. What is the sequence of the tripeptide produced upon treatment with chymotrypsin? Fill each blank with the three-letter designation of the amino acid residues from the N-terminus to the C-terminus.
Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-A
Determine the primary structure of pentadecapeptide X, based on the following results. A). Reagent: merchapthoethanol Released two fragments, namely: 1. pentapeptide (Y), amino acid composition: cys, phe, ser, thr, val 2. decapeptide (Z), amino acid composition: ala(2), cys, leu, lys, phe, pro, tyr, B). Process: Edman Degradation 1. Nt of peptide Y is ser, 2. Nt of peptide Z is ala. C). Enzyme: Carboxypeptidase A 1. val was released from peptide Y; 2. no amino acid was released from peptide Z D). Enzyme: Chymotrypsin 1. peptide Y released two fragments with the following amino acid composition. (phe, ser, thr) (cys, val) 2. peptide Z released three fragments with the following amino acid composition 3. val(2) (ala [2], tyr) 10 (cys, phe) (leu, lys, val, pro, val) E). Enzyme: trypsin peptide Z released two fragments with the following amino acid composition ala (2), cys, leu, lys, phe, tyr val (2), pro

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