Draw two different AMINO ACID side chains forming H bond interactions with atoms on the major groove of the structure below. major groove H. •• • H-N° CH3 ••H-N Adenine R Thymine
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Q: secondary structure? O -KPGHP- O-KRKKK- -YFVWT- O-MRLEK-
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Q: H, =0 N-C-C H ČH3 ОН Figure 1. An amino acid HI
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- Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?OThe ligalon ractionf diffet zatón oPaction fouctose is that of glucose bocallse विजो exrsdrs ns o with a amine group amd q cashony hic acid > footonat) pootonute sdefaotonated grouß. a fve-membered oshg instaad of asix= membored hs depatonuta) is Foomed. a bond is Fomed to a casln Caston mstead of to a methy) opoobhated Potonated casbon A de Protonnted, Idepntonat) the caldehyde yooup mosates to a Functionelizad, de fin dinediza) Je fom dionadiza mew fositn a ketone is formed which ane of the Followrs is be associate) fouctose has 6 Caobon ipids? with in the e nhy Tnstead of 5 as is glucose Aonmo auids.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:…
- re aftached in a chain made rA phuephate andr A ba kleane made ef amine and eerboed gipe bee side dine iw fuckhemes ERnEEted ty hase pairs form a desle hdir. hree carboaviie neide are attached in a dyce molesale. the word(s) that best completes the statement 13. A fat that contains omly single bonds is atn) 2 fat. 14. The type of reaction that involves a single ouletaance breaking down into two Or more other substances is alu)2 seaction. 15. The energy carrier of the cell is the compound named 2 L 16. A reaction that can occur without continuing outside help is said to be 2 17. The relationship between the mass before and after a chemical reaction is described by the ? 18. Because it can proceed in either direction, the reaction between hydrogen gas and iodine gas is said to be ?. 19. An electrochemical cell that generates electricity using substances that are continually replenished from an outside source is a(n) ? cell.t-eNA 39 Nucleic Acids Convey Genetic Information inal to carboxy-ter- nthesis Is it asser rase the opp was ane e use 34. Why are weak bonds important to macromolecular structure and enzyme funcuo N. N. N. 0.8. The chemical structure of Coenzyme A contains the following except— a phosphoanhydride moiety. a β-mercaptoethylamine residue. a lipoic acid residue. a pantothenic acid residue. an adenosine-3’- phosphate.
- D raw the full structure of the following tetrapeptide . Label the N terminaland C terminal residues. Phe - Cys - Ser - IleProtease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn EraseNucleic Acids Convey polypeptide c' minal directi This ques similar to t' carboxy-ter- hesis ing synth to direct sis, the Secon yase aft e genetic groups of 44. Why is ATP important to protein function, and how is it used to accomplish this? which st is. The m fatthaei, synthetic able of r ataining r thus mus ucleotid h of mor Cwas the chemis re critir a 1966 ponded han our PROT mine the s tetail sizer
- Select the hydrophobic part of this molecule. Η Η 56, 45 H-O. -C- -C-H C=O C=0 C=0 CH2 CH, ČH2 CH2 CH, CH2 CH2 CH2 ČH2 CH2 CH2 CH2 CH2 CH2 CH2 CH, CH, CH2 CH2 CH2 CH CH2 CH2 CH CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH2 CH, CH2 CH2 CH2 CH2 CH2 CH3 CH3 CH3 Copyright © 2009 Pearson Education, Inc. Selected Coordinates Clear HICiew PDIICH Current Attempt in Progress Glycoproteins that are N-linked to B-rhamnose (see Box 11.B) have been found in archaea and eubacteria. Draw the molecular structure of this linkage with the residue as a monomer at physiological pH. Do not show primary or secondary hydrogens. o OH CH H H * Eclit DrawingH-Bond donors PSA 1532 55 140 60 75 Which of the following compounds is more likely to be a substrate for Pgp: Compound H-Bond acceptors MW Ionization A 350 pKa=3 B 520 pKa=9 CD 400 pKa=4 D 470 pKa=8 4038