Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- a. How many peptide bonds are there? b. How many amino acid residues are there? c. In exact order, identify the name of the amino acids in the peptide chain. d. Give the full name of this peptide. e. Give the 3-letter abbreviation and 1-letter abbreviation. f. Calculate the pI of this peptide.arrow_forwardYou are in the process of determining theamino acid sequence of a peptide. After trypsin digestion followedby the Edman degradation, you see the following peptide fragments:arrow_forward1. 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. inarrow_forward
- Calculate the pI of the peptide KLMRDSP (pKa = 3.5, 3.9, 9.5, 10.0, 12.5).arrow_forwardDraw the peptide at a pH @1 of Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyrarrow_forwardAnswer the following questions based on the structure of the following peptide and the information in the attached table of enzyme activities. M-F-V-W-E-Q-A-P-S-P-L Subjecting this peptide to trypsin would result in OA Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Lys Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Leu OB. Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro-Leu OC. D. Met-Phe-Val-Trp-Glu-Gin-Arg and Pro-Ser-Pro-Lys O E. Met-Phe-Val-Trp and Glu-Gin-Arg-Pro-Ser-Pro-Leuarrow_forward
- 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 yourarrow_forwardExplain the reason why most proteins have less D-aspartate and elastin has increasing levels of D aspartate steadily with age.arrow_forwardIf you were given the abbreviations for 4-6 amino acids, could you draw the polypeptide chain AND determine its isoelectric point? Do this for the amino acid Asp-Arg-Val-Tyr-Ilearrow_forward
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