1. Draw an approximate titration curve of the following amino acid. Label the approximate isoelectric point ofarginine on the curve and be sure to label the axis of the graph appropriately. You DO NOT need to draw thestructure of this amino acid here. Pk1= 1.92, pk2=8.99 and pk3=12.48. Show your work for determining theisoelectric point. You can draw out your curve within the text box or upload a drawing.A▾B I-IB 7

The titration curve is a plot that tracks the behavior of amino acids under the influence of…

Answered: 1. Draw an approximate titration curve…

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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Similar questions

Draw the L enantiomer in a Fischer projection for each amino acid; identify the amino acid as neutral, acidic, or basic. Give the three-letter sign [3], and the one-letter symbol [4].arginine a. arginine b. arginine c. a. glutamic acid b. glutamic acid c. glutamic acidtyrosine b. valine c. arginine
Calculate the isoelectric point for each amino acid.a. asparagine: pKa (COOH) = 2.02; pKa (α-NH3+) = 8.80b. methionine: pKa (COOH) = 2.28; pKa (α-NH3+) = 9.21
For each amino acid: [1] draw the L enantiomer in a Fischer projection; [2] classify the amino acid as neutral, acidic, or basic; [3] give the three-letter symbol; [4] give the one-letter symbol. a. arginine c. glutamic acid b. tyrosine d. valine
Histidine is an amino acid with three titratable groups: an -NH3+ group (pKa = 9.2), a -COOH group (pKa = 1.8), and an imidazole (amine-like) group (pKa = 6.0). The titration curve for histidine is shown below with four points highlighted. (a) Identify which point on the titration curve corresponds to the pKa for each of the titratable groups, and which point corresponds to the pI. Explain your choices. (b) Calculate the value of pI for histidine
A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species
Draw the Fischer projections representing the L forms of the following amino acids at pH higher than their isoelectric point. a) cysteine b) alanine
Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 6% alanine (?r 89.1) by weight. Calculate the approximate molecular weight of bovine cytochrome c if there are 6 alanine residues. Please enter your answer with three significant figures. approximate bovine cytochrome c MW: Da Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 11% serine (?r 105). Calculate how many serine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number. number of serine residues:
Identify and match the lettered regions in the titration curve of a basic amino acid. pic 5.jpg Alpha amino pka Alpha carboxyl pka Imidazole side chain pka Isoelectric point A. D B. A C. B D. C
Based on your knowledge of the natural amino acids, what would you expect pKa of the sidechain of beta-(aminomethyl)succinic acid to be? Draw an appropriate titration curve for beta-(aminomethyl)succinic acid, labeling the axes, indicating the equivalence points and the pKavalues, and use a drawing to show the protonated/deprotonated forms.
5 (a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
How many chiral carbons are present in this amino acid (aqueous form)? (Identify the following amino acid (at pH = 7.0): (COO-)–CH(NH3+)–CH2–CH2–CH2–CH2–(NH3+)) zero chiral carbons one chiral carbon two chiral carbons three chiral carbons four chiral carbons
Tripeptides are composed of three amino acids linked by peptide bonds. Given a set of amino acids, you can make several different tripeptides.(a) Use the three-letter shorthand notations to name all the tripeptides that can be made from serine, tyrosine, and glycine. Each amino acid will be used once in each tripeptide.(b) Draw the complete structure of the tripeptides that have glycine as the N-terminal amino acid.

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