Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at:a. pH 1.0b. pH 10.1

The estimated charge on the given Lys-Ala-His-Asp-Ser peptide is +3.At low pH, the amino acid is…

Answered: Determine the net charge on 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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Hydrolysis of dodecapeptide P with the enzyme trypsin affords the following fragments: Arg, Ser-Tyr-Ser-Met-Lys, Ala-Gly-Asp-Phe-Glu-Arg. Hydrolysis with chymotrypsin yields: Glu-Arg, Arg-Ser-Tyr, Ser-Met-Lys-Ala-Gly-Asp- Phe. What is the amino acid sequence of P? Submit Answer Retry Entire Group 9 more group attempts remaining
The oligopeptide isolated from the brain of an animal has the sequence glu-his-tri-ser-tyr-gly-leu-arg-pro-gly. Determine the total charge of the molecule at pH 3.0; 5.5; 11.0. In what pH range is the isoelectric point of the peptide?
Identify and describe how you would PEGylate this peptide at its N- terminal amine. Discuss the reaction conditions you need to carry out the reaction and explain how pH affect selectivity of reaction. Draw the chemical structure of the resulting mPEG peptide conjugate.
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Make use of the table below in answering the questions asked: Amino acid pK₁ pK₂ pK, Isoleucine 2.32 9.76 Leucine 2.32 9.74 Lysine 2.16 9.06 10.54 Tyrosine 2.20 9.21 10.46 1. Kindly draw manually the structure of tripeptic ILY at pH 7.00 2. Kindly draw manually the most protonated structure of tripeptide ILY
The skeletal structures of the two amino acids, glycine and lysine, are given below along with the values of the relevant acid dissociation constants (pKa). NH,* PK, - 10.79 - HạN*CH2CO,¯ S pK¸=2.35 (CH2)4 - H3N*CHCO,- pK,=9,78 lysine (Lys) glycine (Gly) pK, = 9.18 pK, - 2.16 For an aqueous solution of glycine alone, calculate the value of pH at which the ratio of the concentration of neutral glycine zwitterions to the concentration of protonated cation is 102. On your under each of the following conditions. In the blank, provide the total charge of the dipeptide. (Example: If the charge is two plus write the answer simply as 2, if the charge is negative two write the answer as -2). draw the skeletal structure of the dipeptide, Lys-Gly, when it is solvated in an aque us solution i. pH= 1 ii. pH= 12
you have isolated the following peptide: His-Ser-Arg- Ala-Glu- Leu- Pro- Gly Calculate the approximate charge of the peptide at Ph 1, 3, 5, 8, 11, 14 AND what is the PI of this peptide?
Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a. pH 1.5 b. pH 8 c. pH 13
Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residue
Hemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. 1. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer. This process is not 100% efficient, so we may have leftovers of dimers and monomers. In the graph given, can we label the peaks given as a tetramer, dimer, or monomer?
the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.

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Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH 10.1