Amino acid Ala Asp Arg Cys a-carboxyl group a-amino group pK a pK a 2.35 9.78 1.99 9.90 1.82 8.99 1.92 10.7 R-group pK 3.90 12.48 8.37
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Chemistry
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- H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14BIM-46187 is a protein inhibitor that binds to the a-subunit of the G. protein. It prevents the GDP/GTP exchange and prevents activity of the G protein. Which of the following would you expect to see lower levels of as a result? You can select more than or answer. S-S NH2 Mol. M: 795.11 Image: https://aobious.com/aobious/protein-inhibitors/1086-bim-46187.html Select one or more: O a. Cyclic AMP (CAMP) O b. Tyrosine kinase O . HSP O d. Adenylyl Cyclase (AC) O e. DAG O f. JAK O g. IP3Subjecting this peptide to trypsin would result in L-M-F-V-W-E-Q-A-P-S-P O A. Lys and Met-Phe-Val-Trp-Glu-Gln-Arg and Pro-Ser-Pro OB, Leu-Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gln-Arg-Pro-Ser-Pro OC. Op. Lys and Met-Phe-Val-Trp-Glu-Gln-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro OE.
- Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsinL-Ala -NAM-NAG-NAM-NAG L-Ala D-Glu D-Ala DA Transpeptidase D-Ala DAP I D-Ala D-Glu I L-Ala NAG-NAM-NAG-NAM 21. Modification of the enzyme pictured (above) might result in resistance to A. quinolone B. streptomycin C. chloramphenicol D. penicillin E. trimethoprimThe primary structure of b-endorphin, a peptide containing 31 amino acids synthesized by the body to control pain, is shown here: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr- Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu What fragments are obtained as a result of treatment withcyanogen bromide?
- The primary structure of b-endorphin, a peptide containing 31 amino acids synthesized by the body to control pain, is shown here: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr- Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu What fragments are obtained as a result of treatment with trypsin?Cut the following protein with the Serine Proteolytic enzyme Trypsin. How many peptide fragments are present after the protein is treated with Trypsin? Val-lle-Arg-Lys-Leu-Arg-Gly-Ala-Lys-lle 6. 10The figure shows interaction of various amino acids (Phe, Arg, and Asn) present in Hb with 2,3-DPG. The side chains of these amino acids and 2,3-DPG interactions are circled in red. HO Но Phe HN Asn H2N NH Arg You identify a mutant version of the globin chain where the Arg in circle 2 is replaced with aspartic acid in a patient. Would the Hb protein in this patient be able to transport oxygen even in the presence of 2,3-DPG? ASPARTIC ACID (asp) No, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind oxygen and not 2,3 DPG
- Consider the positively charged amino acid lysine Lys2+ 21 COOH I H&N-C-H I pH 14 12 10 8 6 4 2 0 CH₂ I CH₂ I CH₂ I CH₂ T NH₂+ 0 Nelson p85 2.18 = 2.18 PK₁ Lys+ COO™ I H₂N-C-H H₂N-C-H ī I -----) 8.95 Lysº 8.95 pK₂ pka carboxyl = 2.19 pkaamino = 9.67 pka sidechain = 4.25 COO™ I CH₂ I CH₂ I CH₂ I CH₂ I NH₂¹ 1.0 2.0 Equivalents of OH added- COO™ I H₂N-C-H I 10.79 1 10.79 pk Isoelectric point Lys CH₂2 I CH₂ I CH₂ I CH₂ T NH₂ 3.0 +H3N NH3+ T CH₂ T CH₂ CH₂ CH₂ -COO™ H Lysine (Lys, K) Physiological pH = 7.4 < pl → Amino acid is positively charged at physiological pH 1. Consider glutamate in its fully protonated form (e.g. in a pH = 1 solution) 1) Draw all the forms of glutamate at various pH 2) Calculate the pl of this amino acid 3) Sketch a titration curve showing pH as a function of added [OH-] and locate the predominant forms of histidine in the curve STEPS: 1. Find the H atoms that can be removed on the molecule 2. Associated a pka value to each removable H. 3. Draw the Aa structure at:…Answer 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-LeuNAZO 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