how to use valine in a 2 chemical equation involved in this experiment using the scheme below .
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how to use valine in a 2 chemical equation involved in this experiment using the scheme below .
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- E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o opQLSeysIVg8-5-v0riWm3uEQ4RUA3Hdua_NDMQI25SST619X-KVA/viewform What makes alanine a nonpolar, neutral amino acid? O The presence of a chiral carbon O The hydrocarbon group attached O The zwitterion cannot be formed due to nonpolarity O The acid and base groups neutralizes the side chains What is NOT true about hemoglobin? It is a fibrous protein that helps oxygen combine with carbon It has an iron atom inside the structure It contains four polypeptide units O It transports oxygen to the different cells in the body27. 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 phosphorylated
- N- HO sta on e yor current pH the peptide? Explain your yor a) Based the charge state shown, what is a possible vahe amswer wsi'ng 2-3 sentences. Show the qull pH ramge yor this protonation otate 6) Hypo thesize a oingle amino acid substitution Cmutation) that wonld make Your amswer must include the which residue this lic You. peptide more hydrophi you would mutate and what new re sidue would take its place Include a 1 sentence explanation g your reasoning yourExamine 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.Thr-Lys-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys Write the sequence using one-letter abbreviations. sequence: TLPIVAPMGYGK Incorrect Estimate the net charge on the peptide at pH 7. charge at pH 7: +1 Estimate the net charge on the peptide at pH 12. charge at pH 12: 0 Incorrect
- Chymotrypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: C-1 G-A-E-A-T-E C-2 G-K-V-G-A-H-A-G-E-Y C-3 V-L-S-P-A-K-T-N-V-K-A-A-W What is the sequence for the peptide? NOTE: Label the fragments when reconstructing the peptide chain e.g. for trypsin T-1, T-2 etc...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; 1,7,121.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…
- Which of the peptide sequences below best matches the hydropathy plot shown? 5 10 15 Residue Number ILYYAGSREDHSGYLIL EQSDTERNQHGALIYLI LIFLAIFPAGSTSEDRR RAFLILFMTYFLILFLI LHGDQNRERDGHSQERD 2 Hydropathy value 0 -4 -2Which of the peptide sequences below best matches the hydropathy plot shown? L 10 Residue Number 4 2 Hydropathy value -2 0 セー RAFLILFMTYFLILFLI ILYYAGSREDHSGYLIL OLHGDQNRERDGHSQERD EQSDTERNQHGALIYLI 01 5 15Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a. pH 1.5 b. pH 8 c. pH 13