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- a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).b. Please draw the structure of the polypeptide: threonine-lysine-glutamine-valine at pH 7.0, and identify the alpha carbons. C. Estimate the isoelectric point of the polypeptide in (b.)?Briefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)
- a. Use three-letter amino acid abbreviations to write the representation for the tripeptide shown here. i H₂N-CH-C-N-CH-C-N-CH-C-0- CH₂ H -NH H ī CH₂ SH -CH-C-0- CH-OH CH3 b. Give the full name of the amino acid at the C-terminal end of this tripeptide. H₂N-CH-C-N-CH-C-N-CH-C-O- -CH-C-N-CH-C CH₂ c-o- CH₂ OH1. To determine the sequence of amino acids in protein, partial hydrolyses at different points are made and then compared to other sets of partial hydrolyses For example: Complete hydrolysis gave: Phenylalanine-1 Histidine-2 Glutamic acid-1 Leucine - 4 Asparagine-1 Cystine -2 Glutamine-1 Glycine - 2 The Partial Hydrolyses yielded the following: 1st Hydrolysis : 4 polypeptides ● . IA: phe-val-asn-gln-his-leu IB: IC: leu-tyr-leu-val ID: val-cys-gly 2nd Hydrolysis: 3 polypeptides IIA: phe-val-asn-gIn-his-leu-cys-gly-ser-his-leu IIB: val-glu-ala-leu-tyr-leu IIC: val-cys-gly Write down the primary structure of this polypeptide by finding the overlaps of the amino acids therein: Serine-1 Valine-3 Alanine-1 tyrosine-1 cys-gly-ser-his-leu-val-glu-alaTreatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.
- Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide.D. Draw the structure of Histidine and Imidazole. Why do you think we use Imidazole to elute the protein? Why do we use a 6X His tag?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 13
- (a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 0 0 0-2 O +1Please ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?