Draw the structure of Arg - Lys - Ser - Trp at ph 7.4
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- draw the structure of the peptide Asp - Asn-Ser-Lys-Pro at PH 8A synthetic polypeptid made up of L-glutamic acid residues is in a random coil configuration at pH 7.0 but changes to alpha helical when the pH is lowered to 2.0. Explain this pH-dependent conformational transition.what would the net charge on the tetra peptide of sequence ala-lys-glu-ser at ph 7.2 what would it be if the amino group of the Lys residue has been acetylated?
- Draw the structure of the tri-peptide Leu-Asn-Ser at pH 7.4. Use wedges and dashes around the alpha-carbons, and indicate charges where appropriate. Indicate which amino acid(s) has an R group that would avoid water.A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.
- Draw the full structure of the one predominant form of val-asp-asp-arg fragment as it would exist at pH 7.4? Note: Its side chain will also be protonated at that pH.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. 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.
- draw the structure of the tripeptife Pro-Ser-Cys as it would appear at physiological PH with its C-terminal amino acid residue protected as its methyl esterIdentify the structure of the predominant form of the pentapeptide at pH = 12 if there is a pentapeptide Ile-Lys-Asp-Phe-Gly2.2 Aspirin reacts with the amino acid Serine. What is the structure of serine? Draw the structure of the tetra peptide Arg-Lys-Ser-Trp at physiological pH.