Concept explainers
Interpretation:
The
Concept Introduction:
Acid-base properties of Amino acids:
Every amino acid has a carbonyl group and an amino group, and each group can exist in an acidic form or a basic form, depending on
The compound exists primarily in the acidic form in solutions that are more acidic than their
Zwitter ion has both positive as well as negative charge, thus it is also called neutral dipolar ion.
Zwitter ion accepts proton in acidic condition and in basic condition zwitter ion lose electrons.
Isoelectric point are the
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Essential Organic Chemistry, Global Edition
- The maximum number of amino acid side chains that can potentially form an ionic bond (+lIE- interaction) with the side chain of His is _at pH 21;at pH 7 and_at pH 11.5 andat pH 13.5. (assume no partial charges, only +/- whole number integers) 00: 2; 3:1 01:2:4:1 O2:2;3;0 00:2;3:0 00:2, 4:0 00:0: 2: 2 O none of thesearrow_forwardCan you please answer sub questions A and B and show all of the steps please and thank youarrow_forwardThe maximum number of amino acid side chains that can potentially form an ionic bond (+ll- interaction) with the side chain of His is _at pH 21;at pH 7 and at pH 11.5 andat pH 13.5. (assume no partial charges, only +/- whole number integers) 00: 2; 3:1 01:2:4:1 O 2;2;3,0 O 0: 2; 3;0 00:2; 4: 0 00: 0; 2; 2 none of thesearrow_forward
- . Describe the pH range of acceptable buffering behavior for the amino acids alanine, histidine, aspartic acid, and lysine.arrow_forwardSelect the correct representation of this aminoacid in aqueous solution at the stated pH values. pKa (a-CO₂H) = 2.20 pK₂ (α-NH₂) = 9.11 pKa (side chain OH) = 10.07 pl = 5.63 HO Lont out on on OH OH NH₂ NH₂ NH₁ HO NH₂ B D at pH 1 HO NH₂ of of an OH NH₂ NH₂ NH3 O E F G at pH 9.59 at pH 13. at pH 5.63 (the isoelectric point) HO OH HO [Choose ] [Choose ] [Choose ] [Choose ] an NH3 H OHarrow_forwardGive detailed Solution with explanation needed..don't give Handwritten answerarrow_forward
- What is the name of this oligopeptide? Use the three letter and one letter nomenclature of the amino acids. Based on the charges on the peptide, what is the closest pH range would you expect that this was in? 2 to 4? 6 to 8? 10 to 12?arrow_forwardplease explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?arrow_forwardAll amino acids have two ionizable functional groups: an α‑amino group (average p?a of 9.4) and an α‑carboxylic acid group (average p?a of 2.2). Aspartic acid has an ionizable side chain (R group) with a p?a of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. The protonated form of the R group of aspartic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the p?a of the R group and the pH of the solution. Select all the pH values at which the charged form of the R group would predominate.arrow_forward
- a) if maltose is made up of two a-D-glucose units connected together by an a(1->4) linkage, how can it give a positive test as a reducing sugar in a pH=7 solutions such as Fehlings'? b) if a person produces and excudes a polyunsaturated oil from their skin, how does it ultimately make clothes smell bad, and how does baking soda remove the odor? (DETAILS!!! pH neutralizing is not enough!!) c) opioids are compounds derived from opium, which comes from the opium poppy. Although in reality, all poppies produce opioids, the drug "morphine", codeine as well as other opioid pain killers are typically derived from opium. A quick way to find or identify these compounds is to look for a six-membered ring containing a nitrogen. Often, if you see a six-membered ring with a nitrogen, you have some sort of an opioid or a modified synthetic painkiller. With that said morphine and codeine are typically not injected or given orally inpure form. Instead their salts are used, such as morphine sulfate…arrow_forwardQuestion 6 of 25 > Modify lysine to show the predominant form at pH 7. Modify the amino acid by adding or removing atoms or bonds and by adding charges where appropriate. Select Draw Rings More N 0 H / || III C H-O || C ▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬ H H I C *一£一£一£一£ H H I N-H Erase Q2 Qarrow_forwardA1c Select ONE peptide linkage and draw a circle around all of the atoms that would lie in a single plane. H R2 | H H;Ñ. || C. N R, H H R3 H Ilt. O=0arrow_forward
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