3. Draw representations of each of the following amino acids in the given solution. Amino acid and solution Your Answer Histidine, above the pl Asparagine, below the pl Proline, at the pl
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- 27. Draw palmitic acid, identify a, B and w carbons, write out its short hand notation 28. Examine the peptide sequence below and then answer the questions: H2N-Gly- Leu- Ala-Asp-Cys-Asn-Trp-lle-Ser-Phe-Lys-Cys-Arg-Pro-coOH a. Circle the asparagine residue b. A possible intramolecular disulfide bond can be formed within this peptide between which two residues? c. Circle one residue which has a positively charged side chain under pH 7.4 d. Circle one residue which has a negatively charged side chain under pH 7.4 e. Circle the residue which can be phosphorylated4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".2) For the following amino acids, encircle those with a net charge of -2 at high pH underline those with +2 at low pH Aspartic acid, Alanine, Arginine, Glutamic acid, Valine, Leucine, Lysine, Isoleucine
- 6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…4. What is the net charge (approximately) on the polypeptide shown below at pH 12.5? Lys - Arg - Val-Cys - Glu1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
- 1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…Please don't provid3e handwritten solution ....1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
- A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separationExamine the peptide. Thr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑LysThr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑Lys Write the sequence using one‑letter abbreviations. Estimate the net charge on the peptide at pH 7. Estimate the net charge on the peptide at pH 12.1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
