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 DRAW THE MOLECULAR STRUCTURE AR POLARITY (IS IT POLAR OR NONPOLAR?) MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
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- &. How many milldiners of a 2wv Lidocaine HCI stock selution in water should be used in preparing 30 ml of a 0.5% wiv Lidocaine HCI solution? . From the following formula for antificial tears, caleulate the quantity of each ingrodient roquired to prepare half donen of the 0ml containers. Poyviny alcohol 149 Povidone Chiorobutanol Serile sodum chioride soution a.%. s to 100 m How many milldiners of water should be added to 60 ml. of a 2% wiv agqueous solution to prepare a 1% wiv solution?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…NAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12
- 1. List down the amino acids in the following format Amino Acid Physiological Significance 3 letter Code 1 letter code Chemical Structure 2. List down the different qualitative and quantitative tests for Amino Acids Test Reagents Principle Positive Reaction/ResultCan a tablet be sufficient in neutralizing a 100 mL of stomach acid with a pH of 1.50? Hint: H+ concentration is antilog(-pH). Answer it by YES or NO, why?Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
- a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explainok-Personal Microsoft Edge com/maildeeplink 021 pdt Download Print Save to OneDrive 1. Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in aqueous solution at pH3D10.3. (Relevant pka values are: 2.2 4.3, 6.0, 9.8, and 10.1) Acp is adiusted toTitration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.
- 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 phosphorylatedExamine 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.The peptlde bradykinln is a nonapeptlde. Give the name of the peptide (shown below) by namlng the amlno aclds from the N-terminal to the C- terminal. Use the long name, the 3-letter abbreviation and the 1-letter abbreviation. What is the pl of this peptide? Name Compositon Fxnction LOcalizatio Bradykinl Inflammatio Different n and H N vasodilation Cells HNH n Animal H. HNH H NH он HN N HO