tyrosine 3) Sketch the titration curve for apertic acid. Be sure to labeleach pk.. the f 2. zwittesión, and draw the dominant forms of the amino acid along the curve just ke your lab report, the lecture slides and Figure 3.7 on page 69 of your textbook.
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- 6 (a) A decapeptide has the following amino acid composition: Ala2 , 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. From the experimental data, deduce the primary structure of the decapeptide. (b) Suggest a scheme you will follow to synthesize the dipeptide Ala-GlyThe peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's titration curve. Part b) What would the pI of the peptide be around?Calculate the pI for the following peptide: Phe-Lys-Glu-Asp-Lys-Ser-Ala (note: there is only one alpha carboxyl at the C terminus and one alpha amino group at the N terminus and don't forget to take into account the ionizable side chain groups)
- Consider N-acetyl-d-glucosamine Q.) Draw a chair conformation for the a- and b-pyranose forms of this monosaccharide.Taurine (2-aminoethanesulfonic acid) is sometimes called an amino acid. (a) Explain why this designation is not valid. (b) From which of the 20 standard amino acids is taurine derived? Describe the chemical change(s) that occurred.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).
- Rotation about the peptide bond in glycylglycine ishindered. Draw the resonance forms of the peptide bondand explain why.Consider Isoleucine, structures are provided for the 4 stereoisomers, complete the table by assessing the R/S Configuration and assign appropriate Amino Acid name, choices are: L-Isoleucine, L-Allo Isoleucine, D-Isoleucine, D-Allo IsoleucinePro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.
- Optical isomerism of amino acids. L and D amino acids. Chiral centers of amino acids. Give examples of amino acids that do not have optical isomers.Identify the structure of the predominant form of the pentapeptide at pH = 12 if there is a pentapeptide Ile-Lys-Asp-Phe-GlyApamine is a small protein toxin present in the venom of the honeybee. Ithas the sequenceCNCKAPETALCARRCQQH(a) If apamine does not react with iodoacetate (see Tools of Biochemistry5B), then how many disulfide bonds are present?(b) If trypsin cleavage gave two peptides, then where is(are) the S¬Sbond(s)?
