Please give explanation of answer. Peptides can be separated according to their charges via an ion-exchange column.In a cation-exchange column at pH 3.0, which peptide would elute last?a peptide that contains mostly Lys and Vala peptide that contains mostly Asp and Glu residuesa peptide that contains mostly Tyr and Trp residuesa peptide that contains mostly Ala and Glya peptide that contains mostly His and Arg residues

Ion exchange chromatography is used to separate molecules based on the charge. Anion and cation…

Answered: Peptides can be separated according to…

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

Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Val
Which peptide in below pair has side chains that exhibit predominantly van der Waals forces? Tyr–Asp–Leu–Lys–His or Phe–Asn–Leu–Leu–Met
Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net charge
Which of these peptides is the most hydrophobic? A. KFYV B. ERSC C. PIMF
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
Given below are sequences of amino acids present in an oligo-peptide chain. Count the overall chargeof each assigned peptide and write it in your answer. Along with it also mention that toward swhichelectrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Val
At pH 7.0, in what order would the following three peptides (described by their amino acid composition) be eluted from a column filled with a cationexchange polymer?Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.Peptide B: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.Peptide C: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%
This diagram shows the allowed rotations about the backbone of a peptide: Sigmoidal Curve Homology Matrix Ramachandran Plot BLOSUM
You have a mixture of peptides (RE; EQ; DW; EE; KG). Which peptide will bind most strongly in a column filled with anionite at pH 6.0? Which peptide will bind most strongly to a column packed with a cation at pH 6.0?
What is the overall charge on peptide AVGDWESKELLE at pH 7.0? a. -3 b. -2 c. 0 d. +1 Which of these decapeptide is the most hydrophobic? 1. ADEEEHNRQL 2. AVLKTIFYRS 3. AVLTIIFYRG 4. AVLTDNQLPK
a. The graph to the right displays the degree of helicity that was measured for a peptide as nine additional amino acids were sequentially added to the initial amino acid. Describe the reasons that the helicity curve takes the shape that it does as amino acids are added on to the small peptide.
Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.

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