A. Write the structure of the pentapeptide GLDSC.B. What is the complete name of this pentapeptide?Show a tertiary structure of ACGGC after adisulfide bond forms.A sample of an unknown peptide was divided intotwo aliquots. One aliquot was treated with trypsin;the other was treated with cyanogen bromide.Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce thesequence of the original peptide.Trypsin treatmentAsn-Thr-Trp-Met-lle-LysGly-Tyr-Met-Gin-PheVal-Leu-Gly-Met-Ser-ArgCyanogen bromide treatmentGin-PheVal-Leu-Gly-Metlle-Lys-Gly-Tyr-MetSer-Arg-Asn-Thr-Trp-Met

A) Pentapeptide GLDSC contains five amino acids i.e, glycine, leucine, aspartic acid, serine, and…

Answered: A Write the structure of the…

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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b) The methyl group at the C terminus of aspartame can be cleaved by concentrated sulfuric acid (conc. H₂SO4) to reveal the carboxylic acid (compound 1), which has a pK₂ of 2.43. OH NH₂ OCH3 conc. H₂SO4 OH NH₂ OH Compound 1 The other two pKa values in the molecule are unchanged. It is useful to calculate the isoelectric point (pl) when planning to separate charged species from neutral species with electrophoresis. pKal + PK₂2 2 pl = HINT: i) Calculate the isoelectric point of aspartame. ii) Calculate the isoelectric point of compound 1 and explain your reasoning behind the calculation.
Part B Consider the partial hydrolysis of the peptide Ala-Ser-Gly-Met-Thr-Val. Sort the smaller peptides according to whether they are are likely to form or if they will not form at all during this process. Drag each item to the appropriate bin. • View Available Hint(s) Reset Help Ala-Ser-Gly-Met-Thr Met-Thr-Val Ala-Ser-Gly-Met Ala-Met-Thr Gly-Met-Val Ser-Gly Gly-Met-Thr-Val Gly-Thr-Val Gly-Val Ser-Gly-Met-Thr-Val Likely to form Will not form
Write the structure of all possible peptides containing these amino acids: Ala, Leu, Use single letter abbreviations and capital letters only; i.e. GYR, not Gly-Tyr-Arg. If there are fewer than 6 peptides, leave an appropriate number of answer boxes empty.
(a) An aliphatic aminoglycoside is relatively stable to base, but it is quickly hydrolyzed bydilute acid. Propose a mechanism for the acid-catalyzed hydrolysis.NHHCH2RR2NH2 + sugarRHHOH OHOH Oan aliphatic ribosideH3O+ +(b) Ribonucleosides are not so easily hydrolyzed, requiring relatively strong acid.Using your mechanism for part (a), show why cytidine and adenosine (for example)are not so readily hydrolyzed. Explain why this stability is important for livingorganisms.
The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N > C) A-F-R-M-Y-A. a) Although not listed here, what amino acids might be present at the section connecting the two anti-parallel (turn) strands? NH3" Nterminus
A decapeptide has the following amino acid composition:Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, ValPartial hydrolysis yields the following tripeptides:Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly.Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. Fromthe experimental data, suggest a scheme you will follow to synthesize the dipeptide Ala-Gly
The shaded area in the following diagram shows CH₂ CH | H CO-H-N N-H-O -CH₂ C-OH-N Gly 193 H RN Covalent bond formation between a catalytic amino acid residue and the substrate during chymotrypsin catalysis. Acid-base catalysis by a catalytic residue in chymotrypsin. Oxyanion hole which stabilizes substrate binding in chymotrypsin catalysis. Oxyanion hole which stabilizes transition state in chymotrypsin catalysis. Low barrier hydrogen bond formation between the transition state and one of the catalytic residues of chymotrypsin. ?
For the following peptide there are [ Select] acids present and [ Select] + H3N carbons present? Make sure to check the sidechains for chiral carbons as well. SH amino ◆ chiral H N 00 OO
Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-

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