Chapter 3 Practice Problems Flashcards
(15 cards)
The term specific activity differs from the term activity in that specific activity:
-is the activity (enzyme units) of a specific protein
-is measured only under optimal conditions
-refers to proteins other than enzymes
-refers only to a purified protein
-is the activity (enzyme units) in a milligram of protein
-is the activity (enzyme units) in a milligram of protein
Which two amino acids differ from each other by only one atom?
Ser and Thr
Ser and Cys
Leu and Ile
Ala and Ser
Asp and Asn
Ser and Cys
Of the 20 standard amino acids, only ___ is not optically active. The reason is that its side chain ___.
Lysine: contains only nitrogen
Proline: forms a covalent bond with the amino group
Glycine: is unbranched
Glycine: is a hydrogen atom
Alanine: is a simple methyl group
Glycine: is a hydrogen atom
Which of the following statements about aromatic amino acids is correct?
-The presence of a ring structure in its R group determines whether or not an amino acid is aromatic
-On a molar bases, tryptophan absorbs more ultraviolet light than tyrosine
-All are strongly hydrophilic
-The major contribution to the characteristic absorption of light at 280 nm by proteins is the phenylalanine R group
-Histidine’s ring structure results in its being categorized as aromatic or basic, depending on pH
-On a molar bases, tryptophan absorbs more ultraviolet light than tyrosine
The formation of a peptide bond between two amino acids is an example of a(n) ___ reaction
condensation
isomerization
cleavage
oxidation-reduction
group transfer
condensation
Two amino acids of the standard 20 contain sulfur atoms. They are:
methionine and cysteine
cysteine and threonine
threonine and serine
methionine and serine
cysteine and serine
methionine and cysteine
At the isoelectric pH of a tetrapeptide:
there are four ionic charges
the amino and carboxyl termini are not charged
two internal amino acids of the tetrapeptide cannot have ionizable R groups
only the amino and carboxyl termini contribute charge
the total net charge is zero
the total net charge is zero
By adding SDS (sodium dodecyl sulfate) during the electrophoresis of proteins, is it possible to:
determine a protein’s isoelectric point
determine the amino acid composition of the protein
separate proteins exclusively on the basis of molecular weight
preserve a protein’s native structure and biological activity
determine an enzyme’s specific activity
separate proteins exclusively on the basis of molecular weight
At pH 7.0 converting a proline to hydroxyproline, will have what effect on the overall charge of the protein containing it?
It will stay the same
The answer depends on the salt concentration
It will become more positive
It will become more negative
There is not enough information to answer the question
It will stay the same
Amino acids are ampholytes because they can function as either a(n):
neutral molecule or an ion
standard or nonstandard monomer in proteins
polar or a nonpolar molecule
acid or base
transparent or light-absorbing compound
acid or base
Titration of valine by a strong base, for example, NaOH, reveals two pKs. The titration reaction occurring at pK2 (pK2= 9.62) is:
-COOH + OH- –> -COO- + H2O
-NH3+ + OH- –> -NH2 + H2O
-COOH + -NH2 –> -COO- + -NH2+
-COO- + -NH2+ –> -COOH + -NH2
-NH2 + OH- –> -NH- + H2O
-NH3+ + OH- –> -NH2 + H2O
The functional differences, as well as differences in three-dimensional structures, between two different enzymes from E. coli, result directly from their different:
roles in the metabolism of E. coli
secondary structures
roles in DNA metabolism
amino acid sequences
affinities for ATP
amino acid sequences
In a mixture of the five proteins listed below, which should elute second in size-exclusion (gel-filtration) chromatography>
- cytochrome c Mr= 13,000
- immunoglobulin G Mr= 145,000
- ribonuclease A Mr= 13,700
4, RNA polymerase Mr= 450,000 - serum albumin Mr= 68,500
- immunoglobulin G Mr= 145,000
The uncommon amino acid selenocysteine has an R group with the structure -CH2-SeH (pKa= 5). In an aqueous solution, pH= 7.0, selenocysteine would:
be found in proteins as D-selenocysteine
never be found in a protein
not be optically active
be nonionic
be a fully ionized zwitterion with no net charge
be a fully ionized zwitterion with no net charge
In a highly basic solution, pH= 13, the dominant form of glycine is:
NH2-CH2-COOH
NH3+ - CH2-COOH
NH2-CH3+–COO-
NH3+ –CH2-COO-
NH2-CH2-COO-
NH2-CH2-COO-