Mistakes Flashcards
Up -> serine
Down -> Threonine
Which of the following amino acids have a negatively charged side chain at neutral pH?
Select one or more:
a. Arginine
b. Alanine
c. Asparagine
d. Aspartate
e. Glutamate
d. Aspartate
e. Glutamate
Which of the following amino acids have sulfur-containing side chains?
Select one or more:
a. Histidine
b. Cysteine
c. Methionine
d. Proline
e. Valine
b. Cysteine
c. Methionine
Which amino acid has a guanidine group in its side chain?
Select one:
a. Histidine
b. Lysine
c. Tyrosine
d. Arginine
e. Tryptophan
d. Arginine
Which of the following amino acids have four carbon atoms?
Select one or more:
a. Aspartate
b. Threonine
c. Asparagine
d. Proline
a. Aspartate
b. Threonine
c. Asparagine
Which of the following amino acids have five carbon atoms?
Select one or more:
a. Glutamate
b. Glutamine
c. Histidine
d. Proline
e. Glycine
a. Glutamate
b. Glutamine
d. Proline
Which of the following amino acids have six carbon atoms?
Select one or more:
a. Leucine
b. Isoleucine
c. Histidine
d. Proline
e. Glycine
a. Leucine
b. Isoleucine
c. Histidine
Pair the amino acids with their character! 1. Proline 2. Arginine 3. Glutamate
a. neutral b. acidic c. basic
Select one:
a. 1-a, 2-c, 3-b
b. 1-a, 2-b, 3-c
c. 1-b, 2-c, 3-a
d. 1-b, 2-a, 3-c
e. 1-c, 2-a, 3-b
a. 1-a, 2-c, 3-b
Select the correct statements! I
Select one or more:
a. Acidic amino acids have a net negative charge at neutral pH.
b. The isoelectric point of acidic amino acids is at acidic pH.
c. The isoelectric point of the acidic amino acids can be calculated as the average of their three pKa values.
d. Asparagine is an acidic amino acid.
a. Acidic amino acids have a net negative charge at neutral pH.
b. The isoelectric point of acidic amino acids is at acidic pH.
What is the dominant form of Arginine at pH 6.0? (pKa values of Arginine are 2.2, 9.0 and 12.5).
Select one:
a. Two positive and one negative charges
b. One positive and two negative charges
c. One negative and one positive charges
d. One negative charge e. One positive charge
a. Two positive and one negative charges
(Why?
1st deprotonation of alpha carboxyl group.
=> Arginine is a basic amino acid
=> (-) deprotonated alpha-carboxyl group; (+) R chain; (+) alpha-amino group
=> 2 (+) & 1 (-)
What is the dominant form of Glutamate at pH 7.0?
(pKa values of Glutamate are 2.2, 5.6 and 9.2).
Select one:
a. One negative charge
b. One negative and one positive charges
c. One positive and two negative charges
d. One positive charge
c. One positive and two negative charges
What is the dominant form of Histidine at pH 8.0? (pKa values of Histidine are 1.8, 6.0 and 9.2).
Select one:
a. One positive and one negative charges
b. Two negative and one positive charges
c. One negative charge
d. One positive charge
a. One positive and one negative charges
Select the correct statements!
Select one or more:
a. Glutamate has a negative charge on its side chain at the isoelectric pH.
b. Glutamate has a negative charge on its side chain at neutral pH.
c. Arginine has a positive charge on its side chain at the isoelectric pH.
d. Arginine has a positive charge on its side chain at neutral pH.
b. Glutamate has a negative charge on its side chain at neutral pH.
c. Arginine has a positive charge on its side chain at the isoelectric pH.
d. Arginine has a positive charge on its side chain at neutral pH.
( A is incorrect -> at isoelectric point, the deprotonation of side chain does not occur before the next pKa value)
Which of the following statements are true for the isoelectric form of amino acids?
Select one or more:
a. All the naturally occurring amino acids have one positive and one negative charges.
b. The a-amino group of all the naturally occurring amino acids has a positive charge.
c. The a-carboxyl group of all the naturally occurring amino acids has a negative charge.
All are correct
(at isoelectric point, the a-amino group is not deprotonated and have (+), whereas deprotonated carboxyl group ihas (-)
=> net charge = 0 (aka isoelectric point)
At neutral pH a tetrapeptide of glycylalanylarginylglutamate has…
Select one:
a. two positive and three negative charges
b. two positive and one negative charges
c. one positive and one negative charges
d. one positive and two negative charges
e. two positive and two negative charges
e. two positive and two negative charges
(glycine has a free amino group => (+)
Glutamate has a free carboxyl group = 1 (-)
Glutamate is acidic => 1 (-)
Arginine is basic => 1 (+)
The bonds between amino acids => 0 charge
=> Total = 2 (+) & 2 (-) )
The arginyllysylaspartate tripeptide has
Select one or more:
a. its isoelectric point at basic pH.
b. three positive and two negative charges at neutral pH.
c. two positive and two negative charges at its isoelectric point
All are correct
this tripeptide has 2 basic aa => pKI is basic
The chirality of an amino acid results from the fact that its a—carbon…
Select one:
a. is bonded to four different chemical groups.
b. is a carboxylic acid.
c. is symmetric.
d. is in the L absolute configuration in naturally occurring proteins.
e. has no net charge.
a. is bonded to four different chemical groups.
For amino acids with neutral side chain, at any pH below the pI of the amino acid, the population of amino acids in solution will:
Select one:
a. have a net positive charge.
b. have no charged groups.
c. have no net charge.
d. have positive and negative charges in equal concentration.
e. have a net negative charge.
a. have a net positive charge.
because of protonated alpha amino group
An octapeptide composed of four repeating glycylalanyl units has:
Select one:
a. a single free amino group on an alanyl residue.
b. two free amino and two free carboxyl groups.
c. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue
d. two free carboxyl groups, both on glycyl residues.
e. a single free amino group on an alanyl residue and a single free carboxyl group on a glycyl residue.
c. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue
The backbone of two amino acid residues in a protein can be described as (where Ca is C-alpha):
Select one:
a. Ca–C–N–Ca–C–N
b. Ca–N–Ca–C–Ca–N–Ca–C
c. Ca–N–C–C–N–Ca–
d. C–N–Ca–Ca–C–N
e. Ca–Ca–C–N–Ca–Ca–C
a. Ca–C–N–Ca–C–N
By adding SDS (sodium dodecyl sulfate) during the electrophoresis of proteins, it is possible to:
Select one:
a. preserve a protein’s native structure and biological activity
b. separate proteins exclusively on the basis of molecular weight.
c. determine a protein’s isoelectric point.
d. determine the amino acid composition of the protein.
e. determine an enzyme’s specific activity.
b. separate proteins exclusively on the basis of molecular weight.
Specific enzyme activity:
Select one:
a. is the enzyme activity (expressed as units'') of a specific protein.
b. is the enzyme activity (enzyme as
units’’) in a milligram of protein.
c. is the enzyme activity (expressed as ``units’’) in a mol of protein.
d. refers to proteins other than enzymes.
e. refers only to purified proteins.
b. is the enzyme activity (enzyme as ``units’’) in a milligram of protein.
In the a helix the hydrogen bonds:
Select one:
a. occur only between some of the amino acids of the helix.
b. occur mainly between electronegative atoms of the R groups.
c. are perpendicular to the axis of the helix.
d. occur mainly between electronegative atoms of the backbone.
e. occur only near the amino and carboxyl termini of the helix.
d. occur mainly between electronegative atoms of the backbone.
Thr and/or Leu residues tend to disrupt an a-helix when they occur next to each other in a protein because:
Select one:
a. of the possible covalent interactions between the Thr and/or Leu side chains.
b. both amino acids are highly hydrophobic.
c. the R group of neither amino acid can form a hydrogen bond.
d. of electrostatic repulsion between the Thr and/or Leu side chains.
e. of steric hindrance between the bulky Thr and/or Leu side chains
e. of steric hindrance between the bulky Thr and/or Leu side chains
( This is when a large group in a molecule makes reactions not work)
Amino acid residues commonly found at the end of b turn are:
Select one:
a. Pro and Gly.
b. Ala and Gly.
c. two Cys.
d. hydrophobic.
e. those with ionized R groups.
a. Pro and Gly.
(Proline alpha-imino group cannot form H-bond => cause a break/kink
Glycine does not have beta carbon)
A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro- Gly-. The sequence is most probably part of:
Select one:
a. b turn.
b. parallel b sheet.
c. a helix.
d. a–sheet.
a. b turn.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are:
Select one:
a. restricted to only about seven of the twenty standard amino acids found in proteins
b. always side by side.
c. generally on different polypeptide strands.
d. generally near the polypeptide chain’s amino terminus or carboxyl terminus.
e. generally near each other in sequence.
e. generally near each other in sequence.
Which of the following statements is false?
Select one:
a. a-keratin is a protein in which the polypeptides are mainly in the a-helix conformation
b. Silk fibroin is a protein in which the polypeptide is almost entirely in the b conformation.
c. Collagen is a protein in which the polypeptides are mainly in the a-helix conformation
d. Gly residues are particularly abundant in collagen.
e. Mutations in collagen have been shown to be responsible for some human diseases
c. Collagen is a protein in which the polypeptides are mainly in the a-helix conformation
(single collagen polypeptides -> left handed helices
3 collagen polypeptide bundles -> right-handed helix)
To alter the shape of the a-keratin chains–as in hair waving– the a-keratin chains have undergone one chemical step resulting the conversion of disulfide bridges to Cysteine. What subsequent steps are required?
Select one:
a. chemical reduction and then chemical oxidation
b. chemical oxidation and then shape remodeling
c. shape remodeling and then chemical reduction
d. shape remodeling and then chemical oxidation
e. chemical reduction and then shape remodeling
d. shape remodeling and then chemical oxidation
When oxygen binds to a heme-containing protein, the two open coordination bonds of Fe2+ are occupied by:
Select one:
a. two O2 molecules.
b. two O atoms.
c. one O2 molecule and one heme atom.
d. one O2 molecule and one amino acid atom.
e. one O atom and one amino acid atom.
d. one O2 molecule and one amino acid atom.
In haemoglobin, the transition from T state to R state (low to high affinity) is triggered by:
Select one:
a. subunit dissociation. b. oxygen binding.
c. Fe2+ binding.
d. heme binding.
e. subunit association.
b. oxygen binding.
Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?
Select one:
a. It is normally found associated with the haemoglobin molecules that are
extracted from red blood cells.
b. It decreases the affinity of haemoglobin for oxygen.
c. It binds to the heme groups of haemoglobin.
d. It is an allosteric modulator.
e. It binds with lower affinity to foetal haemoglobin than to adult haemoglobin.
c. It binds to the heme groups of haemoglobin.
binds to the central compartment of the hemoglobin tetrame
To calculate the turnover number of an enzyme you need to know the:
Select one or more:
a. initial velocity of the catalyzed reaction at low [S].
b. initial velocity of the catalyzed reaction at [S]»_space; KM.
c. KM for the substrate.
d. enzyme concentration.
b. initial velocity of the catalyzed reaction at [S]»_space; KM.
d. enzyme concentration.
Enzyme X exhibits maximum activity at pH = 6.9. X shows a fairly sharp decrease in its activity when the pH goes much lower than 6.4. One likely interpretation of this pH activity is that:
Select one:
a. the enzyme is found in gastric secretions
b. a Lysine residue on the enzyme is involved in the reaction.
c. a Glutamate residue on the enzyme is involved in the reaction.
d. a Histidine residue on the enzyme is involved in the reaction.
e. the enzyme has a metallic cofactor.
d. a Histidine residue on the enzyme is involved in the reaction.
A good transition-state analog:
Select one:
a. binds to the enzyme more tightly than the substrate.
b. binds covalently to the enzyme.
c. is too unstable to isolate.
d. binds very weakly to the enzyme.
e. does not react with the native enzyme
a. binds to the enzyme more tightly than the substrate.