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Test: Amino Acids, Peptides, Proteins - MCAT MCQ


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10 Questions MCQ Test Organic Chemistry for MCAT - Test: Amino Acids, Peptides, Proteins

Test: Amino Acids, Peptides, Proteins for MCAT 2024 is part of Organic Chemistry for MCAT preparation. The Test: Amino Acids, Peptides, Proteins questions and answers have been prepared according to the MCAT exam syllabus.The Test: Amino Acids, Peptides, Proteins MCQs are made for MCAT 2024 Exam. Find important definitions, questions, notes, meanings, examples, exercises, MCQs and online tests for Test: Amino Acids, Peptides, Proteins below.
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Test: Amino Acids, Peptides, Proteins - Question 1

Which of the following amino acids has a net negative charge at physiologic pH (~7.4)?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 1
  • Amino acids with acidic side groups carry a net negative charge at physiologic pH.
  • Glutamate (glutamic acid) has a side group containing a carboxylic acid.
  • Glutamate has a net negative charge at physiologic pH.
Test: Amino Acids, Peptides, Proteins - Question 2

A polypeptide with a net positive charge at physiologic pH (~7.4) most likely contains amino acids with R groups of what type?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 2
  • At physiologic pH, basic functional groups will be protonated, attaining a positive charge.
  • Aliphatic R groups are saturated hydrocarbons.
  • A polypeptide with a net positive charge at physiologic pH most likely has a basic R group.
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Test: Amino Acids, Peptides, Proteins - Question 3

The amino acids in hemoglobin (or any protein) uniformly have which of the following configurations?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 3
  • Configurations (either relative or absolute) in amino acids refers to the stereochemical configuration around the chiral carbon.
  • Due to differences in the priority of different amino acid side chains, not all amino acids have the same "Absolute Configuration", which refers the R/S naming convention. Some amino acids are R, and some are S.
  • However, all amino acids have the same "Relative Configuration", which refers to the D/L naming convention. All biologically produced amino acids are in the L configuration.
Test: Amino Acids, Peptides, Proteins - Question 4

Which of the following properties of a protein is least likely to be affected by changes in pH?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 4
  • Primary structure is the amino acid sequence of a protein plus the peptide bonds joining them together.
  • Change in pH are unlikely to alter amino acid sequence or break peptide bonds.
  • The primary structure of a protein is least likely to be affected by changes in pH.
Test: Amino Acids, Peptides, Proteins - Question 5

Hydrogen bonding between separate subunits of DNA polymerase is an example of which of the following?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 5
  • 1 degree structure through 3 degree structure have to do with individual polypeptides.
  • 4 degree structure refers to the global three dimensional arrangements found in multi-subunit proteins.
  • Hydrogen bonding between separate subunits of DNA polymerase is an example of 4 degree structure.
Test: Amino Acids, Peptides, Proteins - Question 6

The unique cyclic structure of which of the following amino acids plays a central role in the formation of alpha helices and beta sheets?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 6
  • Alpha helices and beta sheets are two three dimensional motifs that regularly appear in local segments of amino acids.
  • Proline has a unique cyclic structure which differentiates it from the other common amino acids.
  • Proline plays a central role in the FORMATION of alpha helices and beta sheets. While proline's unique structure may also disrupt both alpha helixes and beta sheets, it's ability to make sharp turns facilitates the FORMATION of both structures, with proline commonly being found at the beginning of alpha helices or at the turns in beta sheets.
Test: Amino Acids, Peptides, Proteins - Question 7

Electrophoretic separation of leucine from a protein sample would be least effective at which of the following pH values?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 7
  • Leucine has an aliphatic side chain.
  • At physiological pH, leucine exists as a zwitterion.
  • Electrophoretic separation of leucine from a protein sample would be least effective at pH 7.4.
Test: Amino Acids, Peptides, Proteins - Question 8

Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?
(Note: the isoelectric point of each polypeptide occurs at pH 6)

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 8
  • The isoelectric point for a polypeptide is the pH at which the molecule does not have a net charge.
  • Electrophoretic separation depends on the existence of a negative net charge.
  • None of the polypeptides would move at pH 6.
Test: Amino Acids, Peptides, Proteins - Question 9

The alpha helix is an example of which of the following structural properties of proteins?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 9
  • Secondary structure refers to the three dimensional arrangement of small segments of amino acids in a polypeptide.
  • The alpha helix is three dimensional arrangement of amino acids in a polypeptide, where the chain takes on a telephone-cord-like shape.
  • The alpha helix is an example of secondary structure.
Test: Amino Acids, Peptides, Proteins - Question 10

All hydrophobic amino acids (valine, leucine, isoleucine, etc.) share which of the following properties?

Detailed Solution for Test: Amino Acids, Peptides, Proteins - Question 10
  • Hydrophobic amino acids prefer to minimize their interactions with water molecules.
  • Polar, acidic, and basic R groups all share partial or full charges, which interact favorably with polar water molecules.
  • All hydrophobic amino acids share nonpolar uncharged R groups.
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