What is the significance of the blue regions of the following molecule? Me Me pe steroid skeleton Me O None of the answers O They are prone to metabolism, thus limiting the lifetime of the drug O They introduce a dipole moment to the molecule allowing the correct alignment of binding groups when the molecule binds to the binding site O They represent the skeleton of acetylcholine O They are polar groups that increase water solubility
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- The following structure is more active than morphine as an analgesic. H3C N. CH3 H. H3C O .. What is the principal reason for this? O The extra acetyl group binds to cell surface receptors improving active internalization. O The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. O The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. O The acetyl groups increase the stability of the drug in the cellular environment. O ..The following structure is more active than morphine as an analgesic. H3C CH3 H. H3C' O Il.. What is the principal reason for this? The extra acetyl group binds to cell surface receptors improving active internalization. The acetyl groups mask a polar group allowing the structure to cross the blood brain barrier more efficiently. The extra acetyl group masks an alcohol group which would otherwise undergo a phase Il metabolic conjugation reaction leading to rapid excretion of the drug. The acetyl groups increase the stability of the drug in the cellular environment. O Il..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 group
- Acetylcholine is inactivated by the enzyme acetylcholinesterase. Which amino acid residue's side chain plays an important role as an acid-base catalyst in the enzyme's mechanism of action? O Glycine O Lysine Histidine Alanine O AsparagineWhich of these heterocyclic drugs is likely to be the least soluble in water? Use the Fsp³ parameter to decide. OH Tramadol Chemical Formula: C16H25NO2 YOUR OW Pantoprazole Torasemide Chemical Formula: C16H15F2N3O4S Chemical Formula: C16H20N4O3S Temazepam -OH Chemical Formula: C16H13CIN₂O2 Tioconazole Chemical Formula: C16H13C3N₂OS A. Tramadol B. Pantoprazole C. Torasemide D. Temazepam E. ToconazoleWhich of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts The transition state contains at least one partial bond. QUESTION 12 The angle o in a peptide best describes: O the angle between the two peptide bonds O the angle between the alpha carbon (Ca) and the amide O the angle between the alpha carbon (Ca) and the carbonyl O the angle between the alpha carbon (Ca) and its side chain QUESTION 13 Investigating how protein subunits come together studies: super- secondary structure Click Save and Submit to save and submit. Click Save All Ansuers to save all anscers 7977 Mostly cloody
- Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides 1. Ile—Val—Cys—Arg—Thr—Gly—Cys—Lys—Asn—Phe—Leu2. Trp—Lys—Cys—Phe—Arg—His—Thr—Lys—Cys—SerTreatment of the intact polypeptide with trypsin yields fragments with the following aminoacid compositions(Arg, Cys2, Ile, Ser, Val)(Arg, Cys2, Gly, Lys, Thr, Phe)(Asn, Leu, Phe)(His, Lys, Thr)(Lys, Trp)Edmands chemistry reveal the following PTH derivatives in equal quantity after cycle 1• PTH--Ile and PTH--Trp a) Rewrite the intact polypeptide, by indicating the positions of the disulfide bonds(Indicate your reasoning) b) How many products do you expect after chymotrypsin cleavage of the intactpolypeptide? c) You are performing an isoelectric focusing experiment (IEF) on a gel with a pH range of 2to 14. Indicate on the diagram below at what point along the gel will peptide 1 abovefocus, in the presence (X) and absence (Y) of DTT. (also show your calculations)Regarding the mechanism of action of chymotrypsin, the formation of a strong hydrogen bond with the hydroxyl group (serine amino acid) increase its: Basicity Nucleophilicity All the answers are correct Electron densityAllosteric inhibitors of hemoglobin will decrease enzyme activity (oxygen binding) through which of the following mechanisms? Binding the enzyme in "T" conformation and displacing an activator Binding the enzyme and enhancing the Vmax Binding the enzyme, and keeping it in the "R" conformation Binding the enzyme, and keeping it in the "T" conformation
- Give the product of this reaction sequence: NH3* Bg-CH3 Bg SH (cobalamin) Adenosyl-S H₂C-NH OH A Adenosyl-O intermediate D HN-CH3 Adenosyl-NH HS SH B ATP O-CH3 PPP₁ H3C-S+ Adenosyl H₂N E Adenosyl-O product OH с NH₂ S-CH3please show DETAILED mechanism and I will upvote: biotin carboxylase Ö— NH N-carboxyblotin O-C-OH + ATP bicarbonateOne of the following glycosaminoglycans is anti-coagulant O Heparan sulphate O Hyaluronic acid O Heparin sulphate O Keratan sulphate O Chondroitin sulfate search