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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Match the following antibiotics with the drug strategy that would provide resistance to them. rifampin which blocks transcription [ Choose ] Choose] tetracycline which misaligns the beta-lactamase anticodon to its codon mutation of the TRNA binding site of the ribosome penicillin which blocks peptidoglycan creation of alternate metabolic pathway that ultimately leads to the same product synthesis mutation of RNA polymerase polymyxin which causes leakage in the porin which removes drug from periplasmic space cell membrane sulfonamide which inhibits enzyme of [Choose ] folic acid synthesis pathway Question 14 2 pts % & 5 7
The peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this process, the products that are generated are: O PTH-Leu, PTH Cys, PTH-Arg. PTH-Ser, PTH-GIn, and PTH-Met O PTH-Leu-Cys-Arg-Ser-Gin-Met O PTH-Met and Leu-Cys-Arg-Ser-Gin-Met O PTH-Leu-Cys and PTH-Arg-Ser-Gin-Met O PTH-Leu and Cys-Arg-Ser-Gln-Met
A lipase enzyme has been isolated from a bacterium with a strong red color, found in industrial waste from a fishing company. This enzyme has great potential for elaboration of degreasers for industrial use as it can work at a wide range of temperature (between 4 ° and 80 ° C). However, it is estimated that its purity for industrial purposes is only 35% since it is contaminated with a low molecular weight protein that binds the smallest red pigment peptides and salts product of the purification process 1- Propose a methodology to increase the degree of purity of this enzyme, eliminatingsmall proteins and color.2- How it is ensured that the degree of purity of the enzyme has increased.
I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?
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What does it mean when a person is lactose intolerant? Biologically, what causes this? How can it temporarily be treated?
Why are protein synthesis inhibitors typically broad spectrum? What might prevent a protein synthesis inhibitor from being broad-spectrum?
Please depict a noncovalent interaction important for the function of lysozyme.
The properties of a side chain can be affected by its microenvironment, or the environment that is in the immediate vicinity. For example, the Lys side chain can become slightly more basic its protonated form can be stabilized by its microenvironment. Which of the following microenvironments do you expect to increase the basicity of Lys? O A microenvironment that is composed of hydrophobic residues. O A microenvironment composed of lipid molecules O A microenvironment composed of positively charged side chains. O A microenvironment composed of negatively charged residues.
Discuss the role of feedback inhibition in the anabolism ofpurine-containing nucleotides.
In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacid
You are presented with Cytidine 5' triphosphate and Thymidine 5' triphosphate. Draw and upload to Efundi these phosphorylated structures as they would be connected in a polinucleotide in the order CpT / Show the individual phosphorylated structures first then show how they combine to form the polynuleotide. Show at any one of these structures where the glycosidic bond occurs

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