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Part 1 - Final Examination

Quiz by Ailynn Vel Rayos

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25 questions
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  • Q1
    The "Tails" of the molecules in the figure orient away from water. Which of the following describes the tail's movement away from water?
    Polar
    Adhesive
    Hydrophobic
    Hydrophilic
    60s
  • Q2
    Of the 20 standard amino acids, only ___________ is not optically active. The reason is that its side chain ___________.
    alanine; is a simple methyl group
    glycine; is unbranched
    proline; forms a covalent bond with the amino group
    glycine; is a hydrogen atom
    60s
  • Q3
    Two amino acids of the standard 20 contain sulfur atoms. They are:
    cysteine and threonine.
    cysteine and serine.
    methionine and serine
    methionine and cysteine
    60s
  • Q4
    All of the amino acids that are found in proteins, except for proline, contain a(n):
    carboxyl group.
    ester group.
    amino group.
    carbonyl group.
    60s
  • Q5
    Which of the following statements about aromatic amino acids is correct?
    The major contribution to the characteristic absorption of light at 280 nm by proteins is the phenylalanine R group.
    On a molar basis, tryptophan absorbs more ultraviolet light than tyrosine.
    All are strongly hydrophilic
    Histidine’s ring structure results in its being categorized as aromatic or basic, depending on pH.
    60s
  • Q6
    Which of the following statements about cystine is correct?
    Cystine forms when the —CH2—SH R group is oxidized to form a —CH2—S—S—CH2— disulfide bridge between two cysteines.
    Cystine is an example of a nonstandard amino acid, derived by linking two standard amino acids.
    Cystine is formed by the oxidation of the carboxylic acid group on cysteine.
    Cystine is formed through a peptide linkage between two cysteines.
    60s
  • Q7
    Which of the following molecules make up the basic structure of a cell membrane?
    Phospholipids
    Steroids
    Fatty acids
    Waxes
    60s
  • Q8
    Amino acids are ampholytes because they can function as either a(n):
    acid or a base.
    neutral molecule or an ion.
    standard or a nonstandard monomer in proteins.
    polar or a nonpolar molecule.
    60s
  • Q9
    For amino acids with neutral R groups, at any pH below the pI of the amino acid, the population of amino acids in solution will have:
    no charged groups.
    a net negative charge.
    no net charge.
    a net positive charge.
    60s
  • Q10
    At pH 7.0, converting a glutamic acid to -carboxyglutamate, will have what effect on the overall charge of the protein containing it?
    there is not enough information to answer the question.
    it will become more positive.
    it will stay the same.
    it will become more negative
    60s
  • Q11
    At pH 7.0, converting a proline to hydroxyproline, will have what effect on the overall charge of the protein containing it?
    there is not enough information to answer the question.
    it will stay the same.
    it will become more positive.
    it will become more negative
    60s
  • Q12
    The formation of a peptide bond between two amino acids is an example of a(n) ______________ reaction
    group transfer
    isomerization
    oxidation reduction
    condensation
    60s
  • Q13
    The peptide alanylglutamylglycylalanylleucine has:
    five peptide bonds.
    no free carboxyl group.
    a disulfide bridge.
    four peptide bonds.
    60s
  • Q14
    An octapeptide composed of four repeating glycylalanyl units has:
    one free amino group on a glycyl residue and one free carboxyl group on an alanyl residue.
    one free amino group on an alanyl residue and one free carboxyl group on a glycyl residue.
    one free amino group on an alanyl residue.
    two free amino and two free carboxyl groups.
    60s
  • Q15
    Which of the following is correct with respect to the amino acid composition of proteins?
    Larger proteins have a more uniform distribution of amino acids than smaller proteins.
    Proteins contain at least one each of the 20 different standard amino acids.
    Proteins with different functions usually differ significantly in their amino acid composition.
    Proteins with the same molecular weight have the same amino acid composition.
    60s

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