Hydrolysis of a decapeptide yields the following amino acids.ala, asp, arg, his, leu, lyS, met, tyrThe following fragments produced upon subjecting the decapeptide to various enzymatic and chemicahydrolysisSanger's method: DNP-arg and nonapeptideCyanogen bromide. met, leu-asp-his, and hexapeptideTrypsin: arg, ala-lys, and heptapeptideChymotrypsin: tyr, arg-ala-lys-tyr, and pentapeptideCarboxypeptidase: his and nonapeptideDetermine the amino acid sequence of the decapeptide:[ Select 1

sanger's method decapeptide treated with sanger's reagent(1 fluoro 2.4 dinitrobenzene) yeilds…

Answered: Hydrolysis of a decapeptide yields the…

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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In this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOH
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.
There are two competing processes for the manufacture of lactic acid, chemical and biochemical syntheses. The chemical synthesis involves the hydrocyanation of acetaldehyde, while the biochemical synthesis involves the fermentation of sugars or starch. Discuss the TWO advantages and THREE disadvantages of synthesising lactic acid via the biochemical route.
When a nonapeptide undergoes partial hydrolysis, it forms dipeptides, a tripeptide and two tetrapeptideswhose amino acid compositions are shown. Reaction of the intact nonapeptide with Edman’s reagentreleases PTH-Leu. What is the sequence of the nonapeptide?1. Pro, Ser 3. Met, Ala, Leu 5. Glu, Ser, Val, Pro 7. Met, Leu2. Gly, Glu 4. Gly, Ala 6. Glu, Pro, Gly 8. His, Val
In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectively
Unbranched homopolymer of N-acetyl glucosamine is : 1.Cellulose 2.Chitin 3.Curcumin 4.Concanavalin A
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.
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.
Determine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg，Pro, Lys ,Lys ,Met ,Trp，Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide， free Arg ，free Trp. 3）CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.
Psilocybin is a hallucinogenic compound found in some mushrooms. Present a straightforward pathway for its biosynthesis from one of the aromatic amino acids.
Consider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.
Which of the structures below is that of о-в-D-glucopyranosyl-(1->4)- a-D-glucoругanose CH2OH CH2OH H. OH он H Он OH OH CH2OH HOH2Ć OH он CH2OH CH2OH OH H он H он он CH2OH CH2 OH H OH он OH None of the other structures are correct.

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