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- H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.Q: 1.5%. Sucrose by massx M what volume f soft,dmink Solin Noitolu millimeter contain' 5:29 of Suvrose bolovitine 102 102 24A) nioino) 220 ud s d ro tnaroa 220M 220m VWhat is the important values needed to calculat Km and Kcat afor an enzyme data?
- provide brief explanation thnksQuestion 2. While internal cysteine amino acid sidechains in proteins undergo oxidation to produce disulfide crosslinks that stabilize the protein structure after folding, solvent-exposed cysteine sidechains can remain in their reduced thiol form and serve as reactive nucleophiles (recall for instance Acyl Carrier Proteins involved in fatty acid biosynthesis or various oxidoreductase enzymes). The reactive thiol groups in proteins can be detected using Ellman's test, wherein the protein is reacted with a disulfide Ellman's reagent to form a new mixed disulfide and a 2-nitro-5-thiobenzoate (TNB) byproduct. Upon addition of base, TNB is deprotonated to form a dianion, which absorbs light in the visible region and can be detected using UV-Vis spectroscopy. Ellman's Reagent CO₂H -NO₂ internal disulfide crosslink O₂N- HO₂C SH solvent- exposed thiol UV Absorbance at 412 nm O₂N- -S TNB²- alkaline pH O₂N- SH HO₂C 2-nitro-5-thiobenzoate (TNB) -NO2 mixed disulfide CO₂H a) Provide a detailed…All amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Lysine also has an ionizable side chain (R group) with a pK, of about 10.5. One of the possible ionization states of lysine is shown in the image. i H₂N-CH-C-OH CH₂ 1 Incorrect CH₂ CH₂ CH₂ NH₂ At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups. Show Transcribed Text 11.9 S The protonated form of the R group of lysine is shown in the structure. The ratio of the charged (protonated) form to the deprotonated form depends on the pK, of the R group and the pH of the solution. 12.0 10.5 5.4 Select all the pH values at which the charged form of the R group would predominate. 2.2
- Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Entropy change of Go= − 423 kcal/mole of Glucose8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F CloudyEnzyme kinctics a. How to determine Km and Vmax of a-glucosidase enzyme isolated from weathered rice b. Curcumin is expected to inhibit the activity of the a-glucosidase enzyme. How to determine the inhibitory activity of curcumin against a -glucosidase? c. If the results of experiment number 3b are known that curcumin can inhibit a -glucosidase, how to determine the type of inhibitor?
- The mutated form of hemoglobin (hemoglobin S, or HbS) in sickle-cell anemia results from the replacement of a glutamate residue by a valine residue at position 6 in the ß chain of the protein. Normal hemoglobin is designated HbA. Under conditions of low [O₂], HbS aggregates and distorts the red blood cell into a sickle shape. See image of eight aggregated HbS molecules. Sickled red blood cells are relatively inflexible and may clog capillary beds, causing pain and tissue damage. The sickled red blood cells also have a shorter life span, leading to anemia. Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6? arginine phenylalanine Aggregate of HbS molecules lysine leucine alanine Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a B chain ranion located in the interior of the neotain In daaxshamaalahin homauar thic nookat is laastad on the curfona of tha 0H. N- imert) waib)omoatosib owl to erit waib) aemoaloanate ow io H H 12 ( k) CH;NHCH,OCH;CONHCH3 houulifanoo yam as wsid (e1eoet lenonulanos o) leulocR en H. H. c=Ć-C- H. нно о H. онн rplugelomiclinos ns bas lSo 0 H. нн H. H. H H- H-Ć H HNH N H -H H. H. (! H H. H---H H H H. H H H-C-C-C=C-C-C-H HHH H---S-5-5--H H H f) (CH3CH2O)2CO CH3COCH2CO2CH3 b) CH;CHBr(CH2)¿CH(CH3)2 a) CH3(CH2)3CH3 CH3CHCHCH2CHCH2 (CH3)3CCH2CH3 STEREOCHEMISTRY 1. Convert the following condensed and Lewis structures into line-angle structuresWhat is X in the following biochemical pathway? O O O O O NH3 + A. A ош O R CH a-ketoglutarate coenzyme PLP aminotransferase CH3 D. glutamate 0 B. || NH R. X 0™ coenzyme TPP decarboxylase E. 0™ C. CH CO₂ OH O™ R. H 'Н