Draw all possible products of a single hydrolysis being completed on the following polypeptide: Ala-Ser-Met-Ser
Q: Write down the amino acid sequence of the tripeptide shown below. CH3 H H₂N NH -NH,
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Q: Draw the α-l-glucopyranose sugars using Haworth projections:
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Q: Which of the following are known as helix breakers? O Proline Isoleucine leucine O Valine O…
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Q: Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a.…
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- 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 13Note:- Provide detailed explanation for the reaction that involves the removal of nitrogen from an alpha-amino acid, forming an alpha-keto acid. Please explain with the help of an example.gal(α1→6)gal(α1→6)glc(α1↔2β)fru. Which of the complete IUPAC of this tetrasaccharide? α-D-galactopyranosyl-(1→6)-β-D-galactopyranosyl-(1→6)- α-D-glucopyranosyl-(1↔2)-β-fructofuranoside α-D-galactopyranosyl-(1→6)- α-D-galactopyranosyl-(1→6)- α-D-glucopyranosyl-(1↔2)-β-fructofuranoside α-D-galactopyranosyl-(1→6)- α-D-galactopyranosyl-(1→6)- α-D-glucopyranosyl-(1↔2)-β-fructofuranose α-D-galactopyranosyl-(1→6)-β-D-galactopyranosyl-(1→6)- α-D-glucopyranosyl-(1↔2)-β-fructofuranose
- Rotation about the peptide bond in glycylalanine is hindered. Draw the resonance forms of the peptide bond and explain why.15. Rank the solubility of the following fatty acids in water. A. C<E<B<D<F<A B. A<F<D<B<E<C C. C<E<B<F<D<A D. A<D<F<B<E<C 16. Using the same information in no. 15, rank the solubility of the fatty acids in hexane.* A. C<E<B<D<F<A B. A<F<D<B<E<C C. C<E<B<F<D<A D. A<D<F<B<E<CMatching type (Refer to picture) Choices: A, B, C, D, E. F G cyclopentane ring a side chain other than methyl and oxide methyl side chain any ring included in the phenanthrene nucleus
- Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has p?ap�a values of 2.4 (carboxyl group) and 9.7 (amino group).9. H. State if/how Aureliano's mutation changes the amino acid sequence and describe the effect that change has, if any, on the protein.Explain what happens if even one amino acid is substituted for another in a polypeptide chain. Provide a specific example.
- Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminusDraw the following sugars using Haworth projections:a. b-d-galactopyranose b. a-d-tagatopyranose c. a-l-glucopyranoseA. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.
