Complete Solutions.
Which of the following best describes the structure of heme?
-a nicotinamide structure that is readily oxidized
-a negatively charged phosphate group
-a planar porphyrin ring that binds iron
-an n-link glycosylation
A planar porphyrin ring that binds iron
Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of
the following amino acids would not facilitate this type of catalysis?
-valine
-cysteine
-serine
-histidine
Valine
Which of the following proteins is likely to have quaternary structure?
-a protein that contains both a-helix and b-sheet secondary structures
-a multimeric protein that contains multiple peptide chains
-a large transmembrane protein with seven a-helical domains
-a small protein consisting of a single amino acid chain
A multimeric protein that contains multiple peptide chains
Which of the following amino acids would not be commonly found in the middle
of an a-helix?
-valine
-leucine
-tryptophan
-proline
Proline
Both myglobin and hemoglobin contain heme. Myoglobin contains ___ heme
rings. Hemoglobin contains ___ heme rings
-1,4
-1,1
-4,1
-4,4
1 and 4
Which of the following best describes protein domain?
-a linker region between two a-helical structures
-any location on a protein that has a disulfide bond
-a relatively large pattern of three-dimensional structure that is recognized across
many proteins
-a small grouping of secondary structures
A relatively large pattern of 3D structure that is recognized across many proteins
, In the R state, all 4 subunits of hemoglobin exhibit a ___ affinity for oxygen. In the
T state, all 4 subunits exhibit a ___ affinity for oxygen
-High, low
-High, high
-Low, low
-Low, high
High, low
Myoglobin is a ___ protein. Hemoglobin is a ____ protein
-monomeric, tetrameric
-monomeric, monomeric
-tetrameric, tetrameric
-tetrameric, monomeric
-monomeric, tetrameric
Dephosphorylation by a phosphatase requires all of the following except:
-ATP
-Water
-Mg2+
ATP
Competitive inhibitors typically resemble ___
-Active sites
-Substrates
-Cofactors
-Enzymes
Substrates
During noncompetitive inhibition, Vmax is ____
-Decreased
-Increased
-Unchanged
-Saturated
Decreased
During noncompetitive inhibition, KM is ____
-unchanged
-decreased
-increased
-saturated
Unchanged
During competitive inhibition, Vmax is _____
-Increased
-Decreased
-Unchanged
-Saturated
Unchanged
In the Michaelis-Menten equation, velocity (vi) and the Michaelis constant (Km)
are ____ related
-Equally
-Directly