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WorksheetsQuiz 2 and Test 2 Review - BHCM2024 Smr II 2025
Total questions: 50
Worksheet time: 57mins
Which of the following is NOT a function of proteins?
Energy storage
Enzyme catalysis
Structural support
Signal transduction
Which amino acid is achiral?
Alanine
Glycine
Leucine
Serine
At physiological pH (~7.4), which group of amino acids is typically positively charged?
Hydrophobic
Polar
Acidic
Basic
Which of the following amino acids can form disulfide bonds?
Serine
Cysteine
Threonine
Tyrosine
The pKa of the carboxyl group of an amino acid is approximately:
2
5
7
9
Which level of protein structure is defined by the sequence of amino acids?
Primary
Secondary
Tertiary
Quaternary
Which of the following amino acids is a helix breaker?
Alanine
Leucine
Proline
Glutamate
Which protein structure level involves interactions between multiple polypeptide chains?
Primary
Secondary
Tertiary
Quaternary
Which of the following is true about peptide bonds?
They are formed by hydrolysis
They allow free rotation
They are planar and rigid
They are ionic in nature
Which of the following is NOT a noncovalent interaction stabilizing tertiary structure?
Hydrogen bonds
Ionic interactions
Disulfide bonds
Hydrophobic interactions
Which protein structure is most affected by denaturation?
Primary
Secondary
Tertiary
Quaternary
Which of the following is a post-translational modification?
Peptide bond formation
Phosphorylation
Translation
Transcription
Which of the following best describes a zwitterion?
A molecule with no charge
A molecule with both positive and negative charges
A molecule with only positive charge
A molecule with only negative charge
Which of the following is a method used to predict protein structure?
PCR
AlphaFold
Western blot
ELISA
Which of the following amino acids is most likely to be found in the interior of a protein?
Serine
Glutamine
Valine
Arginine
Which of the following is true about metamorphic proteins?
They are always unfolded
They have only one native state
They can adopt multiple functional conformations
They are always denatured
Which of the following best describes the hydrophobic effect?
Attraction between charged groups
Repulsion of water by nonpolar groups
Formation of hydrogen bonds
Disulfide bond formation
All amino acids are chiral.
True
False
The tertiary structure of a protein is stabilized only by covalent bonds
True
False
Explain the defiinitions of and interplay between primary, secondary, tertiary, and quaternary structure in proteins.
The bond that links amino acids together in a protein is called a:
(a)
Explain in detail how two amino acids are bonded together. I'm looking for the type of reaction this is, what product is released, etc.
Explain all of the charges on the amino acid lysine at pH 7.
The (a) value indicates the pH at which a functional group is 50% protonated
How does pH influence the ionization state of amino acids?
An amino acid that has a neutral charge at pH 7 has a +1 charge at pH 5.
Explain:
1. What we know about the pKa of this amino acid
2. What would be the charge of this amino acid at pH 1.5?
3. What would be the charge of this amino acid at pH 11.5?
How do post-translational modifications affect protein function?
Describe what AlphaFold is and how it has transformed protein structure prediction
Which enzyme initiates protein digestion in the stomach?
Trypsin
Pepsin
Chymotrypsin
Amylase
What type of amino acids must be obtained from the diet?
Nonessential
Essential
Conditional
Aromatic
Which organ is primarily responsible for amino acid metabolism?
Kidney
Brain
Liver
Pancreas
Which molecule transports amino acids to the liver?
Hemoglobin
Albumin
Myosin
Insulin
Which vitamin is a precursor for NAD+?
B1
B2
B3
B5
Which enzyme catalyzes the committed step of the urea cycle?
CPSI
ALT
AST
NAG synthase
Which of the following is NOT a function of bile salts?
Emulsify fats
Kill bacteria
Hydrolyze proteins
Denature proteins
Which coenzyme is derived from vitamin B2?
NAD+
FAD
Coenzyme A
Biotin
Which enzyme is used as a diagnostic marker for liver damage?
CPSI
Alanine aminotransferase
Pepsin
Chymotrypsin
Which of the following is true about holoenzymes?
They are inactive
They lack cofactors
They are active
They are vitamins
Explain the relationship between cofactors, apoenzymes, and holoenzymes.
Which molecule is excreted in urine as a result of amino acid metabolism?
Ammonia
Urea
Glucose
Ketone
Which of the following is NOT a feature of enzyme active sites?
Large volume
Excludes water
3D crevice
Noncovalent interactions
Which of the following is a coenzyme?
Mg2+
Zn2+
NAD+
Fe2+
Which of the following is a function of chymotrypsin?
Cleaves nucleic acids
Cleaves oligopeptides
Transports amino acids
Synthesizes urea
(a) is the most abundant protein in the blood.
Bile salts are synthesized from (a)
Explain what the induced conformational model is
How do enzymes lower activation energy?
Explain the difference between competitive, uncompetitive, and noncompetitive inhibitors
Describe the metabolic fate of keto acids derived from amino acids
All enzymes require cofactors
True
False
