(a)
Interpretation: The mechanism for the reaction that adds an Fmoc group to an amino acid under the given conditions is to be drawn.
Concept introduction: Peptide linkage is formed between the amino group of one amino acid and the carboxyl group of other amino acid with the loss of water molecule. Amino acids are naturally occurring compounds in which the amino group is present on the alpha carbon of carboxyl group. The full form of Fmoc is fluorenylmethyloxycarbonyl chloride. It introduces Fmoc group which protects the
(b)
Interpretation: The mechanism for the reaction that removes an Fmoc group from an amino acid under the given conditions is to be drawn.
Concept introduction: Peptide linkage is formed between the amino group of one amino acid and the carboxyl group of other amino acid with the loss of water molecule. Amino acids are naturally occurring compounds in which the amino group is present on the alpha carbon of carboxyl group. The full form of Fmoc
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- According to the paper, F486 is a phenylalanine residue (i.e., an amino acid that is part of a chain that forms a protein) on SARS-CoV-2. It has an important interaction with ACE2 (best seen in Fig. 1(C) and Fig. 2(A)). Looking at this phenylalanine and the green residues surrounding it, which statement best describes the interaction that could be occurring? a) It forms a hydrogen bond with Y83. b) It forms a dipole-dipole interaction with M82. c) It forms London dispersion forces with surrounding residues. d) It encounters repulsions from surrounding residues.arrow_forward1. Type of bond a. H-bond b. Electrostatic interaction c. Hydrophobic bond d. Disulfide bond e. Peptide bond 2. Level of protein structure a. primary b. secondary c. tertiary d. quaternary 3. Method/s of denaturation. choose all that applies a. Heating to 100 degrees Celsius b. Addition of nitric acid c. Reaching Isoelectric point d. Addition of mercuric chloride e. Addition of sulphosalicylic acid f. Addition of alcohol g. Addition of ammonium sulfatearrow_forwardThe peptide structure attached below is most likely a? P.S. Both images are the same.arrow_forward
- 1. (a) Draw a circle around one amino acidin the structure. ( b) Draw a box around one amino acid side chain. (c) Indicate whether the side chain you chose is hydrophobic or hydrophilic. (d) Draw an arrow pointing to a peptide bond 2. If the peptide segment shown above was part of a beta sheet, which of its functional groups would be involved in forming and stabilizing the beta sheet? 3. Which amino acid (also called amino acid residue)would be more likely to occur on the surface of a protein: an aspartate residue or a methionine residue? Explain your choice.arrow_forward(a) An aliphatic aminoglycoside is relatively stable to base, but it is quickly hydrolyzed bydilute acid. Propose a mechanism for the acid-catalyzed hydrolysis.NHHCH2RR2NH2 + sugarRHHOH OHOH Oan aliphatic ribosideH3O+ +(b) Ribonucleosides are not so easily hydrolyzed, requiring relatively strong acid.Using your mechanism for part (a), show why cytidine and adenosine (for example)are not so readily hydrolyzed. Explain why this stability is important for livingorganisms.arrow_forward(a) The isoelectric point (pI) of phenylalanine is pH 5.5. Draw the structure of the major form of phenylalanine at pHvalues of 1, 5.5, and 11.(b) The isoelectric point of histidine is pH 7.6. Draw the structures of the major forms of histidine at pH values of 1, 4,7.6, and 11. Explain why the nitrogen in the histidine ring is a weaker base than the a-amino group.(c) The isoelectric point of glutamic acid is pH 3.2. Draw the structures of the major forms of glutamic acid at pH valuesof 1, 3.2, 7, and 11. Explain why the side-chain carboxylic acid is a weaker acid than the acid group next to thea-carbon atomarrow_forward
- Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.[2] Reaction of the p-nitrophenyl ester with an amino acid ester.a. Why does a p-nitrophenyl ester “activate” the carboxy group of the first amino acid to amide formation? b. Would a p-methoxyphenyl ester perform the same function? Why or why not?arrow_forwardA naturally occurring amino acid such as alanine has a group that is a carboxylic acid and a group that is a protonated amine. a. If the pKa value of a carboxylic acid such as acetic acid is about 5 (see Table 2.1), then why is the pKa value of the carboxylic acid group of alanine so much lower? b. Draw the structure of alanine in a solution at pH = 0. c. Draw the structure of alanine in a solution at physiological pH (pH 7.4). d. Draw the structure of alanine in a solution at pH = 12. e. Is there a pH at which alanine is uncharged (that is, neither group has a charge)? f. At what pH does alanine have no net charge (that is, the amount of negative charge is the same as the amount of positive charge)?arrow_forwardCalculate an approximate pI for Peptide E-G-E-Aarrow_forward
- Show how you would synthesize any of the standard amino acids from each starting material. You may use any necessaryreagents.O(CH3)2CH C COOH(a)CH2CH3(b) CH3 CH CH2 COOH (c) (CH3)2 CH¬CH2¬CHOarrow_forwardExplain why the pKa of the ‒ NH3+ group of an α-amino acid is lower than the pKa of the ammonium ion derived from a 1° amine (RNH3+). For example the pKa of the ‒ NH3+ group of alanine is 9.87 but the pKa of CH3NH3+ is 10.63.arrow_forwardCalculate the isoelectric point for each amino acid. a. cysteine: pKa (COOH) = 2.05; pKa (α-NH3+) = 10.25 b. methionine: pKa (COOH) = 2.28; pKa (α-NH3+) = 9.21arrow_forward
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