Match the columns and choose the correct option. ColumnI Column II AFructose 1 Disaccharide BSucrose 2Monosaccharid Sodium C taurocholate 3Amino acid DGlycine 4Bile salts
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- In the following scheme: HH, H₂C-C-C-Coo II HO H • NH, 1 H₂C-C-C-C000 H 2-Amino-3-ketobutyrate ↓ O H,C-C-CH₂-NH₂ Aminoacetone 0 0 H₂C-C-C-H Methylglyoxal H H₂C-C-COO OH D-Lactate O H₂C-C-C000 Pyruvate What molecule is being metabolized? Identify the reaction at each step. If it is an oxidation-reduction prove this is correct by showing oxidation state changes on the atoms in the structure.Match the following Class of Proteins with their corresponding Prosthetic Group Components. nucleic acids 1. hemoproteins metal ion 2. lipoproteins phosphate group 3. flavoproteins pigment 4. glycoproteins heme unit 5. phosphoproteins 6. nucleoproteins lipid 5. metalloproteins flavin nucleotides -8 chromoprotein carbohydrateConsider 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:…
- 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. inProvide the correct three-letter abbreviation for the following amino acid: Gln ← H₂N-CH-C-C 1 CH3 Ala Arg Asn Asp Cys Glu Gly His lle Leu Lys 包Study the given structures below. Which of the following are epimers? H. H- HO- но H- H- он но H- H- OH HO- но- но H- но- -- но -H но- H- но- HHOH CH;OH H- O- -OH- H- OH CH;OH ČH;OH CHOH D-Gul D-Ido D-Gal D-Tal D-Gul and D-Ido D-ldo and D-Gal D-Gal and D-Tal D-Gul and D-Gal None of the given options
- An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO, H N -C- COOH H O,N CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes. octapeptide sequence: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…Name the compound: 1. Lys-Ile-Met-Val Draw the forms of the amino acid in the solution. 2. Glutamic Acid (4 forms) 3. Lysine (4 forms)