BioChem C785 - WGU - Module 2 - all
Questions and answers already graded
A+| Updated & Verified | 2024
In order to fulfill their function, proteins must fold in proper, 3-D conformations, which molecules,
available in a cell, is likely to help a protein fold properly? - ✔✔chaperone
A misfolded protein can: - ✔✔1. can protein aggregation
2. lose normal function
3. can be degraded by the cell
4. can be the result of denaturation
True about the different levels of protein structure: - ✔✔1. The interactions between the R groups
of the amino acids make up the tertiary level structure of a protein
2. Peptide bonds between amino acids make up the primary structure of a protein
3. Two or more polypeptides each with their own secondary structure and tertiary structures
come together to form a single larger quaternary structure of a protein
, The role that protein structure can play in the disease process: - ✔✔Mutation of an active amino acid
changes an enzymes ability to bind a substrate
Aggregation of the proteins is the main reason behind many neurodegenerative diseases. What
mutations will likely cause a neurodegenerative disease? - ✔✔Replacing a polar amino acid with a non
polar amino acid
Which pair (protein and technique) will likely denature a protein? - ✔✔Hydrogen bonds / ionic bonds:
change in pH
True statements about protein structure and stability: - ✔✔1. Denaturation is the loss of secondary,
tertiary and quaternary structure
2. Ionic bonds between the side chains of the charged amino acids stabilize the protein
3. Denatured proteins retain their primary structure
Alkaline phosphatase is produced by bone and liver in the human body. The amount of alkaline
phosphatase in blood can help identify if a patient potentially has certain types of bone and/or liver-
related disease, including Paget disease, hepatitis, and certain types of cancer. The optimal pH range for
alkaline phosphatase activity is a pH of 8.0 to 10.0. What happens to the activity of the alkaline
phosphatase at a pH of 2? - ✔✔Significantly decreases
Inhibitors that have a similar structure to a substrate of an enzyme are most likely to bind to
the enzyme's active site, and be a competitive inhibitor - ✔✔True
When an inhibitor binds reversibly to a site of the enzyme that is not the active site, what type
of inhibition results? - ✔✔Noncompetitive inhibition
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