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- Write out the sequence of the polypeptide in AA: use the three letter notation, e.g. Met-Ser-Pro-Please draw a single polypeptide chain structure that has the following amino acids (leucine, alanine, cystine, argenine, glutomine, and leucine) as it would appear at physiological pH. Calculate the pl of the polypeptide. I will rate!Indicate which base is (or bases are) the complementarypaired base(s) for each of the following:Adenine ___Cytosine ___Guanine ___Uracil ___Thymine ___
- Draw the titrimetric profile of tyrosine and calculate its isoelectric pHAnswer the questions regarding the tripeptide shown. H3N-CH- -C N-CH-C-N-CH-C-O | CH СНОН H CH2 H3C CH3 CH3 SH Which amino acid is the C-terminal amino acid? threonine cysteine methionine valine What is the name'of this tripeptide, using the three-letter amino acid abbreviations? Capitalize the first let.com/forms/d/e/1 FAlpQLSenLacS5BakgugJMG pBYf0hNjcZaGs2F2MZs4Kn Y10W43JQ/formResponse MCQ Which of the following oligopeptides has net charge equal to zero? O Glutamate - Arginine - Aspartate Lysine O Histidine - Glycine - Tyrosine - Cystine | Glutamate - Alanine - Phenylalanine - Proline O Tryptophan - Methionine - Lysine - Arginine
- Draw the titration curves for the following AA’s: Aspartic acid, Alanine, Lysine, Valine, Serine, and Trrosine.Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…Draw the structure of the following nucleotide: adenosine 3'-monophosphate or guanosine 2-monophosphate
- The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsSuppose that the sequence is part of a larger globular protein. Consider the probable location, either on the external surface or the interior of the protein, of each of the amino acid residues. The table gives the hydropathy index values for selected amino acids in the peptide. Amino acid Hydropathy index alanine 1.8 isoleucine 4.5 threonine -0.7 glutamine -3.5 lysine -3.9 aspartate -3.5Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why not