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Maps Lab Rpt 1-Protein
Draw the product of the reaction shown below. Ignore inorganic
byproducts.
1. NaBH4
2. H3O+
Drawing
CO
Calendar
o
Probl
Atoms,
and F
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- Hemoglobin has pI=6.8. Does hemoglobin have a net negative charge or net positive charge at pH=5.3? At pH=7.3?3a. At right is a hypothetical enzyme that breaks down isoleucine (the amino acid substrate is shown bound in the active site). Identify the specificity residues shown and describe the types of interactions the enzyme uses to select isoleucine as a substrate. b. Give at least two reasons why this enzyme would be less active at very high or very low pH. 0 0 H-0 F CH₂- H₂C NCH;C–CH 1. HNH, OC-CH₂- enzymeCH Post Lab ET O 44 Is saloviglvoyig'lo wouna inenimob stotis W A+H3N-CH-C-OH F CH-CH3 CH3 5. The structure of amino acid valine (Val) is as follows: The pKa for the carboxylic acid group is 2.29; the pKa for the protonated amine group is 9.74. What is the pl value of Val?
- What is the structure that best represents the following amino acid at pH = 10? wolzle H₂N NH₂ O A A HN H₂N B NH₂ i NH₂ OH H₂N C NH3 H₂N NH₂ D OHkamote tops juice Clear selection In this reaction below, the conjugate base of ethanoic acid is H3C-C O-H H20 H3C-C H30 Н20 H30+ CH3COO- CH3COOH Benedict's reagent is used as a test for the presence of reducing sugars. Molisch test Benedict's test Barfood'o TastThe amino acid histidine has ionizable groups with pKą values of 1.8, 6.0, and 9.2, as shown. COOH T H₂N-CH | CH₂ H -O pH UT = ZI Ionizable -COOH group CH H₂N-CH T 1.8 COO- pk₁ CH2 UI COO™ H IZ CH -HisH+ COO™ + H₂N-CH 6.0 pK₂ CH ₂ UI -His H CH -NH COO™ H₂N-CH 9.2 pk3 CH ₂ UI —NH₂ H A biochemist makes up 80 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCl. What is the pH of the resulting solution? CH
- The following is the titration curve of Cysteine. Different charge states of Cys are shown in the table below. Answer the following questions using the information given here. B A Question 6 ů 9 8 Hd 20 21 0€ 52 01 Form 4 Form 3 10 O=O -0--8-- 20 (OH) (equivalents) H&N=CH-C-0 Form 2 -- 1-6-5 05 H₂N-CH-C-OH Form 1 -6-5 SH SH . Which is the most predominant form(s) of Cysteine at the point A on the titration curve? [Select] • Identify which form (among the given above) would Cys assume when the solutions's pH is at its pl [Select] and • Identify the pl (isoelectric point) of this amino acid on the graph: it is marked as [Select] on the graph. Question 7Modify isoleucine to show its structure at pH 1 and pH 13. Modify each amino acid by adding or removing atoms or bonds and by adding charges where appropriate. pH 1 pH 13 Select Draw Rings More Erase Rings More Erase C с CH₂ CH₂ H₂C H₂N 1 CH₂ | CH | 310 H― H O H N U с || 0 H Q2 Q Select Draw / ||| ||| H₂C H₂N 1 CH₂ | CH - n O H | H 0 H N H Q2QShown below is the amino acid tyrosine in its protonated state, with the pK₂of each ionizable proton indicated. pK₂ = 10 HO COOH pk = 9 pK₂ = 2 Which best represents the predominant state of tyrosine at pH 7? a HO. O O OO a b U H3N P H₂N COOH b H₂N COO с НО. H₂N COO d HO. H₂N COO
- This is a worksheet lab - there is no prelab and lab write up is not required Complete the following three tasks below. a. Find the approximate pKa value for each compound in the table below and draw the structure of each compound and its conjugate base. b. Circle the form (the acid or the base) that predominates at a pH of 7. C. Write whether the predominate form would be more water soluble or more organically soluble. (You do not need to show any calculations for this question) Acetic Acid Hydrocyanic Acid pKa = Nitric Acid pKa = Carbonic Acid pKa (1) = (-36 pKa (2) = 10.33 pKa ·0°kcat (sec). 500 A 300 100 80 60 R-Ć- The following kinetic data were obtained for this enzyme: 40 4 H 5 6 COO OH pka: 5.1 and 9.6 7 pH kcat/Km (mM¹ sec) 1000 100 8 9 10 4 B 5 pka: 5.5 and 8.9 6 7 PH R- 8 9 10 KIE (VND) 7 6 5 4 3 نا 2 OH H C 4 5 COO pka 6 - 9.4 7 8 PH 9 10 (i) Draw a scheme showing all the protonation states of E (depicted as E, ES, ESH, EH, EH2, etc.) and their equilibria, together with the actual conversion of S (substrate) into P (product), assuming a single intermediate (you do not have to put in the rate or equilibrium constants). (ii) Match up the 4 pKas in the figures, A and B, with the different protonation states. (Explain what the pKas in Figures A and B represent). (iii) The data in Figure C refers to the kinetic isotope effect on the keat, obtained when the H indicated in red in the reaction given above, is replaced with a deuterium. Why does Figure C show only one pka? Given the information in C, together with that of A and B, what can you conclude about…M Gmail k YouTube Maps Lab Rpt 1-Protein Draw the major product of this reaction. Ignore inorganic byproducts. N H3O+ Drawing >
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