(a)
Interpretation:
At what
Concept Introduction:
The paper electrophoresis is the technique which is used for the separation of amino acids. In this technique, a paper strip coated with a buffer whose
The isoelectric point (
When
(b)
Interpretation:
At what
Concept Introduction:
The paper electrophoresis is the technique which is used for the separation of amino acids. In this technique, a paper strip coated with a buffer whose
The isoelectric point (
When
(c)
Interpretation:
At what
Concept Introduction:
The paper electrophoresis is the technique which is used for the separation of amino acids. In this technique, a paper strip coated with a buffer whose
The isoelectric point (
When the
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Organic Chemistry
- Report the isoelectric point of the peptide, Gly-Asp-Lys-Ile?arrow_forwardConsider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry please highlight the part has been change Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12arrow_forwardThe Arg-Gly-Asp tripeptide (RGD) is a well-known tumour targeting peptidemotif. Explain how you would synthesise H-Arg-Gly-Asp-OH, starting fromthe constituent amino acids? Explain all steps that are necessary and discuss amechanism for one side chain protection and one C terminus protection.arrow_forward
- A decapeptide undergoes partial hydrolysis to give peptides whose amino acid compositions are shown. Reaction of the intact decapeptide with Edman’s reagent releases PTH-Gly. What is the sequence of the decapeptide? 1. Ala, Trp 3. Pro, Val 5. Trp, Ala, Arg 7. Glu, Ala, Leu 2. Val, Pro, Asp 4. Ala, Glu 6. Arg, Gly 8. Met, Pro, Leu, Gluarrow_forwardIllustrate the structure of a peptide with the given sequence below at the given conditions. Serine-Threonine-Glutamic Acid-Lysine-Aspartic Acid-Arginine Form with net charge: +3 Dominant form at pH 7arrow_forwardUsing the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.arrow_forward
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