Agamemnon just got his first octapeptide to sequence. Identify the correct sequence from the data gatheredbelow.He first did a complete acid hydrolysis and identified the amino acids using HPLC. He found he had a lle, Ala, Ser, Asp,Asn, Phe, His, and an Arg.He submitted the octapeptide to conditions of Edman degradation and got the structure below.H.ноHe used carboxypeptidase and generated a His and a heptapeptide.He used chymotrypsin and generated a5-amino acid sequence and a 3-amino acid sequence.He used trypsin and generated a 2-amino acid sequence and a 6-amino acid sequence.Partial hydrolysis of the nonapeptide yielded the fragments RIS, NAH, and SF among others.

The Reactant used in Edman degradation is phenyl isothiocyanate. We know that Edman degradation…

Agamemnon just got his first octapeptide to sequence. Identify the correct sequence from the data gathered below. He first did a complete acid hydrolysis and identified the amino acids using HPLC. He found he had a lle, Ala, Ser, Asp, Asn, Phe, His, and an Arg. He submitted the octapeptide to conditions of Edman degradation and got the structure below. S. HO He used carboxypeptidase and generated a His and a heptapeptide. He used chymotrypsin and generated a 5-amino acid sequence and a 3-amino acid sequence. He used trypsin and generated a 2-amino acid sequence and a 6-amino acid sequence. Partial hydrolysis of the nonapeptide yielded the fragments RIS, NAH, and SF among others.

Agamemnon just got his first octapeptide to sequence. Identify the correct sequence from the data gathered below. He first did a complete acid hydrolysis and identified the amino acids using HPLC. He found he had a lle, Ala, Ser, Asp, Asn, Phe, His, and an Arg. He submitted the octapeptide to conditions of Edman degradation and got the structure below. S. HO He used carboxypeptidase and generated a His and a heptapeptide. He used chymotrypsin and generated a 5-amino acid sequence and a 3-amino acid sequence. He used trypsin and generated a 2-amino acid sequence and a 6-amino acid sequence. Partial hydrolysis of the nonapeptide yielded the fragments RIS, NAH, and SF among others.

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...

See similar textbooks

Similar questions

Draw the structure of the protected amino acid that must be anchored to the solid support in order to use a Merrifield synthesis to prepare leucine enkephalin. Include stereochemistry in your answer. Do NOT explicitly draw any hydrogen atoms in your structure or use abbreviations like OMe, COOH or Ph. (N terminus) Try-Gly-Gly-Phe-Leu (C terminus) НО. H₂N ✔ Edit Drawing H₂C CH₂ OH
10. The following is a PROBLEMATIC solid phase synthesis of the intended tetrapeptide (Gly-Ala-Lys-Val). A) Draw the other TWO tetrapeptides that would result in the box provided. You can abbreviate any of the amino acids using their three lettered codes to save time Resin HO Resin D HF H₂N NH₂ BocHN we (CH₂N Gly-Ala-Lys-Val HO₂C NHBO DCC. pyridine A (CH₂) "NH₂ Resin 1) TFA 2) HO₂C- DCC. pyridine с NHBoc Resi B 1) TFA 2) NHBoc BOCHN HO₂C DCC, pyridine (CH₂) NHBoc (H₂CM) NHDO NHOO B) Fix the incorrect step(s) so as to produce the intended tetrapeptide: Gly-Ala-Lys-Val. You can adapt the reaction scheme accordingly. Steps are lettered for convenience if you are working on paper.
Please show ALL steps and work for this answer. Your help is very much appreciated
For this reaction, a histidine amino acid residue acts as the general base while a lysine amino acid residue acts as the general acid. Draw the arrow-pushing mechanism for this reaction and make sure to include both amino acid residues mentioned above in your mechanism along with their protonation state.
In the following reaction, the purpose of amino acid E193 is to: R, O. -O-P-O-Ad b204 NH, K13 Diminish the metal ion catalytic ability of Mg2*. Accept a proton transfer from S146. Stabilize the positive charge on K13. Anchor Mg2+ in the correct location.
Please explain in depth. I understand it is a zwitterion but I need an in depth explanation. Thank you
lodoacetamides, maleimides, benzyl halides, and bromomethyl ketones can all be used to modify the group on residues. A) amino; basic B) phenyl; Tyr and Trp C) carboxyl; acidic D ) sulfhydryl; Cys E) hydroxyl; Ser and Tyr
7. Determine the net charge at pH 6 on each peptide shown below. The pKa's of relevant side chain functionality are given. The pKa of the NH groups within the backbones of the rings is about 20. pK₂= 10 HO NH3 pk₂ = 11 -NH pK₂=4 HO- NH NH -NH HN HN HN SH pk₂ = 8 Net charge: