molecule 0= FO FO OH OH OH type of molecule (check all that apply) ☐ fatty acid ח ח ח ח monoglyceride diglyceride triglyceride saturated unsaturated ☐ monounsaturated polyunsaturated w-3 w-6 ☐ fatty acid ☐ ☐ ☐ ☐ monoglyceride diglyceride triglyceride saturated unsaturated monounsaturated polyunsaturated w-3 ☐ w-6 fatty acid monoglyceride diglyceride triglyceride saturated ☐ unsaturated ☐ monounsaturated ☐ ☐ ☐ polyunsaturated w-3 ☐ w-6 ✗
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- 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:…draw the structure of a lecithin containing oleic acid and palmitic acid as the fatty acid side chains.Which of the following statements is true In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group O Lipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine
- please show DETAILED mechanism and I will upvote: biotin carboxylase Ö— NH N-carboxyblotin O-C-OH + ATP bicarbonateChoose from A-F. This amino acid may serve as a phosphorylation site, and turn on or off the protein. H3N-C-H H3N-C-H CH2 H2N CH 2 H-C-OH CH2 H2C CH2 CH3 CH3 Choice "A" Choice "B" Choice "C" COO H,N-C-H H,N-C-H H3N-C-H CH2 CH2 C=CH C-NH CH2 NH | CH SH C-N Choice "E" Choice "F" Choice "D"B W S sult, it makes the protein Why is denaturing the proteins necessary for SDS PAGE to work? Use YOUR OWN X mand 3 E D с $ R F 5 Lê 6 T G MacBook Pro B Y H U N J 8 I M 9 K O I O L 44 P command . : 8 ; x { + C option ? I } 1 M
- Which of the following statements is true O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine OLipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood groupProtein Classification A protein is given for each item. Each protein is to be classified based on the required basis of classification. Choose one specific classification for each item. Choices: Fibrous Globular Simple Conjugated Storage Transport Nutrient Defense Regulatory Structural Catalytic Motility1. 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. in
- Serving size 100g % Daily value* Calories ----- Total fat 2g 3.1% Saturated fat 2g ------- Trans fat 0 Cholesterol 0 Sodium 160mg -------- Total CHO 88.25g -------- Dietary fiber 0.01g Sugar content 12g Protein 7.65g *Based on 2000 calories COMPUTATION: CHO, % = 100% – (Moisture+ ash+ protein+ fat) Calorie content pls answer the blanks, thank youẞ-Calendic acid is an omega-6, conjugated fatty acid that is the all-trans isomer of a-calendic acid. HOOC—CH,CH, CH, CH,CH, CH, Part: 0/2 Part 1 of 2 H C=C H C-H H-C H C=C H CH₂ -CH2-CH2-CH2-CH₂ When this fatty acid is partially hydrogenated with one equivalent of H₂ in the presence of a Pd catalyst, a mixture of constitutional isomers is formed. Modify the given structure to draw one of these possible products.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