Just choose from Proteins A-D. Thank you! 1. Protein that will most strongly bind to an anion exchange column:[ Select ]2. Protein that will elute last in gel filtration chromatography:[ Select ]3. Protein that will elute first in hydrophobic interaction chromatography:[ Select ]4. Protein that will elute last in a carbohydrate containing column:[ Select ] Consider a mixture comprised of the following proteins below:-----Charge Affinity to a!!MWProtein;(pH(kDa)7.4)specific %PolarityligandA| 760-3None45B| 300+1Carbohydrate7080-1None60dreamD 55+2None25C.

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: 1. Protein that will most strongly bind…

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

Can you describe the solubility of prolamin, a protein in rice protein bodies, in isopropyl or ethyl alcohol based on its molecular structure?
if the tetrapeptide shown in the binding site above (Gly-Ser-His-lle) were in an aqueous solution at pH=6.2, what fraction of peptide molecules would have a +1 charge?
Sketch the following two tripeptide chains: Asp-Gly-Ser and Ile-Asn-Met at physiological pH . Please provide only typed answer solution no handwritten solution needed allowed
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 which pH range there is the isoelectric point of the peptide?
Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
Let’s consider histidine as a free amino acid in aqueous solution. a) Draw the most likely structure of histidine under biochemical standard state conditions. b) Given that free histidine has the following three pKa values, assign each to its corresponding acidic hydrogen or conjugate base in your structure from part a). pKa1 = 1.7; pKa2 = 6.2; and pKa3 = 9.1 c) For each pKa, give the corresponding expression for the equilibrium constant. It helps to write out the chemical equation for each. d) Create a speciation diagram for histidine by plotting Xi vs pH from pH = 4 to pH = 8 where Xi is the mole fraction of the two histidine species involved in the K2 equilibrium in part c).
The simplest form of the Ramachandran diagram is calculated by ignoring hydrogen bonding, interactions with water, and the hydrophobic effect. Why is this simple form of the diagram still an effective predictor of protein backbone conformation?
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?
Calculate the overall net charge of the following polypeptide at pH = 2.0Gly-Pro-Glu-Asp-Leu-His-Ile-Gln-Asn-Phe A) +1.76 B) -1.76 C) +0.24 D) -0.24
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?
Consider histidine as a free amino acid in aqueous solution. a) Draw the most likely structure of histidine under biochemical standard state conditions. Given that free histidine has the following three pKa values, assign each to its corresponding acidic hydrogen or conjugate base in the structure. pKa1 = 1.7; pKa2 = 6.2; and pKa3 = 9.1 b) For each pKa, give the corresponding expression for the equilibrium constant. It helps to write out the chemical equation for each. c) Create a speciation diagram for histidine by plotting Xi vs pH from pH = 4 to pH = 8 where Xi is the mole fraction of the two histidine species involved in the equilibrium constant in part b).

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