Amino Acids – Nutritional & Structural Classification
1. Which of the following is an essential amino acid?
A. Alanine
B. Serine
C. Valine
D. Glutamate
2. Semi-essential amino acids are those that:
A. Are synthesized in excess amounts
B. Are always required in diet
C. Are required in diet during rapid growth
D. Are not required in diet at all
3. Which of the following amino acids is classified as a non-essential amino acid?
A. Isoleucine
B. Leucine
C. Tyrosine
D. Lysine
4. Which of the following amino acid is an essential amino acid?
A. Serine
B. Tyrosine
C. Phenylalanine
D. Glutamine
5. Which of the following amino acids has a branched-chain structure?
A. Phenylalanine
B. Isoleucine
C. Tryptophan
D. Histidine
6. Aromatic amino acids include all EXCEPT:
A. Tryptophan
B. Tyrosine
C. Phenylalanine
D. Valine
7. Which of the following amino acids contains a sulfur atom?
A. Threonine
B. Methionine
C. Tyrosine
D. Glutamine
8. Basic amino acids are characterized by:
A. Acidic side chains
B. Hydroxyl groups
C. Positively charged side chains at physiological pH
D. Aromatic rings
9. Which of the following is a dicarboxylic (acidic) amino acid?
A. Arginine
B. Glutamic acid
C. Valine
D. Serine
10. Which amino acid has a cyclic structure involving its amino group (an imino acid)?
A. Glycine
B. Alanine
C. Proline
D. Histidine
✅ Answer Key
-
C. Valine
-
C. Are required in diet during rapid growth
-
C. Tyrosine
-
C. Phenylalanine
-
B. Isoleucine
-
D. Valine
-
B. Methionine
-
C. Positively charged side chains at physiological pH
-
B. Glutamic acid
-
C. Proline
Biologically Important Peptides
1. Which of the following is a tripeptide involved in antioxidant defense?
A. Oxytocin
B. Bradykinin
C. Glutathione
D. Vasopressin
2. The main function of oxytocin is:
A. Decreasing blood pressure
B. Increasing urine output
C. Stimulating milk ejection and uterine contraction
D. Promoting glycogenolysis
3. Which peptide hormone is involved in water reabsorption by the kidneys?
A. Oxytocin
B. Vasopressin
C. Bradykinin
D. Glucagon
4. Glutathione is composed of which three amino acids?
A. Glutamate, Cysteine, Glycine
B. Glutamine, Serine, Glycine
C. Aspartate, Cysteine, Alanine
D. Alanine, Cysteine, Glycine
5. Which peptide acts as a vasodilator and increases vascular permeability?
A. Oxytocin
B. Bradykinin
C. Vasopressin
D. Glucagon
6. Which of the following is a nonapeptide involved in childbirth and lactation?
A. Bradykinin
B. Vasopressin
C. Oxytocin
D. Angiotensin II
7. Which peptide helps maintain redox balance in cells?
A. Vasopressin
B. Glutathione
C. Angiotensin
D. Oxytocin
8. Angiotensin II is
A. Tripeptide
B. Pentapeptide
C. Octapeptide
D. Decapeptide
9. Which of the following biologically important peptides is synthesized in the hypothalamus?
A. Glutathione
B. Bradykinin
C. Vasopressin
D. Angiotensin
10. The function of vasopressin is to:
A. Promote water loss
B. Constrict blood vessels and promote water retention
C. Increase insulin secretion
D. Stimulate appetite
✅ Answer Key
-
C. Glutathione
-
C. Stimulating milk ejection and uterine contraction
-
B. Vasopressin
-
A. Glutamate, Cysteine, Glycine
-
B. Bradykinin
-
C. Oxytocin
-
B. Glutathione
-
C. Octapeptide
-
C. Vasopressin
-
B. Constrict blood vessels and promote water retention
Proteins – Functions & Functional Classification
1. Which of the following proteins is classified as a structural protein?
A. Hemoglobin
B. Insulin
C. Collagen
D. Myosin
2. Immunoglobulins are functionally classified as:
A. Regulatory proteins
B. Structural proteins
C. Defensive proteins
D. Transport proteins
3. Hemoglobin functions primarily as a:
A. Hormonal protein
B. Structural protein
C. Transport protein
D. Storage protein
4. Which of the following is a contractile protein?
A. Actin
B. Albumin
C. Keratin
D. Insulin
5. Ferritin is classified as a:
A. Structural protein
B. Storage protein
C. Transport protein
D. Contractile protein
6. Enzymes are functionally classified as:
A. Structural proteins
B. Catalytic proteins
C. Defensive proteins
D. Hormonal proteins
7. Which of the following proteins regulates blood glucose levels?
A. Hemoglobin
B. Myosin
C. Insulin
D. Actin
8. Which of the following is a fibrous protein?
A. Hemoglobin
B. Albumin
C. Myosin
D. Collagen
9. The main function of albumin in blood is:
A. Enzymatic activity
B. Hormone transport
C. Maintaining oncotic pressure
D. Muscle contraction
10. Which of the following proteins plays a role in blood clotting?
A. Thrombin
B. Ferritin
C. Immunoglobulin
D. Keratin
✅ Answer Key
-
C. Collagen
-
C. Defensive proteins
-
C. Transport protein
-
A. Actin
-
B. Storage protein
-
B. Catalytic proteins
-
C. Insulin
-
D. Collagen
-
C. Maintaining oncotic pressure
-
A. Thrombin
Proteins – Definition & Chemical Classification
1. Proteins are composed of which basic building blocks?
A. Fatty acids
B. Nucleotides
C. Monosaccharides
D. Amino acids
2. Proteins are linked together by which type of bond?
A. Glycosidic bond
B. Peptide bond
C. Hydrogen bond
D. Disulfide bond
3. Which of the following is a simple protein?
A. Hemoglobin
B. Casein
C. Albumin
D. Glycoprotein
4. On hydrolysis, simple proteins yield:
A. Only amino acids
B. Amino acids and carbohydrates
C. Amino acids and lipids
D. Amino acids and metals
5. Which of the following is a conjugated protein with a lipid as its prosthetic group?
A. Glycoprotein
B. Lipoprotein
C. Metalloprotein
D. Phosphoprotein
6. Hemoglobin is an example of a:
A. Simple protein
B. Lipoprotein
C. Chromoprotein
D. Glutelin
7. Which of the following proteins contains a phosphate group as a prosthetic group?
A. Casein
B. Albumin
C. Ferritin
D. Globulin
8. Proteins derived by hydrolysis of simple or conjugated proteins are called:
A. Fibrous proteins
B. Conjugated proteins
C. Derived proteins
D. Structural proteins
9. Which of the following is a metalloprotein?
A. Casein
B. Ceruloplasmin
C. Zein
D. Myosin
10. Proteans belongs to which category of proteins?
A. Simple
B. Conjugated
C. Primary Derived
D. Secondary Derived
✅ Answer Key
-
D. Amino acids
-
B. Peptide bond
-
C. Albumin
-
A. Only amino acids
-
B. Lipoprotein
-
C. Chromoprotein
-
A. Casein
-
C. Derived proteins
-
B. Ceruloplasmin
-
C. Primary Derived
Structural Organization of Proteins
1. The primary structure of a protein refers to:
A. α-helix and β-pleated sheets
B. Sequence of amino acids in a polypeptide chain
C. 3D folding of protein
D. Association of multiple polypeptide chains
2. Which type of bond is most important in maintaining the primary structure of proteins?
A. Hydrogen bond
B. Disulfide bond
C. Peptide bond
D. Ionic bond
3. The α-helix is a feature of which level of protein structure?
A. Primary
B. Secondary
C. Tertiary
D. Quaternary
4. Which bond is responsible for maintaining the secondary structure of proteins?
A. Peptide bond
B. Hydrogen bond
C. Disulfide bond
D. Ionic bond
5. Which of the following contributes to the tertiary structure of proteins?
A. Peptide bonds only
B. Hydrogen and ionic bonds
C. Hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges
D. Only disulfide bonds
6. Quaternary structure is seen in proteins that:
A. Are made of a single polypeptide chain
B. Are only found in membranes
C. Have multiple polypeptide subunits
D. Are denatured
7. Hemoglobin is an example of a protein with:
A. Primary structure only
B. Secondary structure only
C. Tertiary structure only
D. Quaternary structure
8. The folding of a single polypeptide chain into a 3D structure represents the:
A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure
9. β-pleated sheet is stabilized mainly by:
A. Ionic bonds
B. Peptide bonds
C. Disulfide bonds
D. Hydrogen bonds
10. Denaturation of a protein affects:
A. Only primary structure
B. Only quaternary structure
C. Secondary, tertiary, and quaternary structures
D. All levels of protein structure
✅ Answer Key
-
B. Sequence of amino acids in a polypeptide chain
-
C. Peptide bond
-
B. Secondary
-
B. Hydrogen bond
-
C. Hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges
-
C. Have multiple polypeptide subunits
-
D. Quaternary structure
-
C. Tertiary structure
-
D. Hydrogen bonds
-
C. Secondary, tertiary, and quaternary structures
Denaturation and Plasma Proteins
1. Protein denaturation involves:
A. Breaking peptide bonds
B. Alteration of primary structure
C. Loss of secondary, tertiary, and quaternary structure
D. Complete hydrolysis of the protein
2. Which of the following agents can cause protein denaturation?
A. Heat
B. Strong acids or bases
C. Alcohol
D. All of the above
3. Denaturation of proteins is usually:
A. Reversible
B. Irreversible
C. Does not affect biological activity
D. Leads to peptide bond formation
4. Which of the following structures is not affected during protein denaturation?
A. Primary
B. Secondary
C. Tertiary
D. Quaternary
5. The major protein responsible for maintaining colloidal osmotic (oncotic) pressure in plasma is:
A. Globulin
B. Fibrinogen
C. Albumin
D. Hemoglobin
6. Which of the following is a function of plasma proteins?
A. Enzyme catalysis
B. Transport of substances
C. Hormone synthesis
D. DNA replication
7. Which plasma protein plays a role in blood clotting?
A. Albumin
B. Globulin
C. Fibrinogen
D. Ceruloplasmin
8. Immunoglobulins belong to which class of plasma proteins?
A. Albumins
B. Globulins
C. Fibrinogen
D. Lipoproteins
9. Plasma differs from serum in that plasma contains:
A. No proteins
B. More electrolytes
C. Fibrinogen
D. Hemoglobin
10. The normal concentration of plasma proteins in human blood is approximately:
A. 2–3 g/dL
B. 4–6 g/dL
C. 6–8 g/dL
D. 10–12 g/dL
✅ Answer Key
-
C. Loss of secondary, tertiary, and quaternary structure
-
D. All of the above
-
B. Irreversible
-
A. Primary
-
C. Albumin
-
B. Transport of substances
-
C. Fibrinogen
-
B. Globulins
-
C. Fibrinogen
-
C. 6–8 g/dL
Digestion and Absorption of Proteins
1. Protein digestion begins in which part of the gastrointestinal tract?
A. Mouth
B. Stomach
C. Small intestine
D. Large intestine
2. The enzyme pepsin is active in:
A. Acidic pH
B. Alkaline pH
C. Neutral pH
D. All pH
3. The zymogen form of pepsin is:
A. Pepsinogen
B. Trypsinogen
C. Chymotrypsin
D. Enteropeptidase
4. Which hormone stimulates the release of gastric juice rich in pepsinogen and HCl?
A. Secretin
B. CCK (Cholecystokinin)
C. Gastrin
D. Somatostatin
5. In the small intestine, the enzyme that activates trypsinogen is:
A. Enterokinase
B. Pepsin
C. Amylase
D. Rennin
6. Which of the following is NOT a brush border enzyme involved in protein digestion?
A. Aminopeptidase
B. Dipeptidase
C. Carboxypeptidase
D. Enteropeptidase
7. End products of protein digestion absorbed in the small intestine are mainly:
A. Whole proteins
B. Polypeptides
C. Amino acids and dipeptides
D. Triglycerides
8. Absorption of amino acids occurs mainly in the:
A. Stomach
B. Duodenum and jejunum
C. Colon
D. Esophagus
9. Transport of amino acids across intestinal mucosa is primarily:
A. Passive diffusion
B. Simple diffusion
C. Secondary active transport with sodium
D. Primary active transport with potassium
10. In infants, the enzyme that helps in curdling milk is:
A. Pepsin
B. Trypsin
C. Rennin (Chymosin)
D. Elastase
✅ Answer Key
-
B. Stomach
-
A. Acidic pH
-
A. Pepsinogen
-
C. Gastrin
-
A. Enterokinase
-
C. Carboxypeptidase
-
C. Amino acids and dipeptides
-
B. Duodenum and jejunum
-
C. Secondary active transport with sodium
-
C. Rennin (Chymosin)
Urea Cycle, Disorders & Significance
1. The urea cycle primarily takes place in the:
A. Kidney
B. Brain
C. Liver
D. Intestine
2. The first step of the urea cycle occurs in which part of the cell?
A. Cytosol
B. Endoplasmic reticulum
C. Nucleus
D. Mitochondria
3. Which of the following is the first enzyme of the urea cycle?
A. Argininosuccinate synthetase
B. Ornithine transcarbamoylase
C. Carbamoyl phosphate synthetase I
D. Arginase
4. Which of the following molecules is directly converted into urea in the final step of the cycle?
A. Citrulline
B. Arginine
C. Ornithine
D. Aspartate
5. Which of the following is an allosteric activator of Carbamoyl Phosphate Synthetase I?
A. Citrulline
B. N-Acetylglutamate (NAG)
C. Urea
D. Aspartate
6. Inherited deficiency of ornithine transcarbamoylase leads to accumulation of:
A. Ammonia
B. Urea
C. Glucose
D. Creatinine
7. Which of the following is a key function of the urea cycle?
A. Fat synthesis
B. Removal of carbon dioxide
C. Detoxification of ammonia
D. Hemoglobin production
8. Urea is transported from the liver to the kidneys via:
A. Bile
B. Lymph
C. Portal vein
D. Bloodstream
9. Hyperammonemia is dangerous primarily because it:
A. Causes dehydration
B. Leads to hyperglycemia
C. Is neurotoxic and can cause coma
D. Increases RBC production
10. Which urea cycle disorder is X-linked recessive in inheritance?
A. Argininosuccinate lyase deficiency
B. Carbamoyl phosphate synthetase I deficiency
C. Ornithine transcarbamoylase deficiency
D. Argininemia
✅ Answer Key
-
C. Liver
-
D. Mitochondria
-
C. Carbamoyl phosphate synthetase I
-
B. Arginine
-
B. N-Acetylglutamate (NAG)
-
A. Ammonia
-
C. Detoxification of ammonia
-
D. Bloodstream
-
C. Is neurotoxic and can cause coma
-
C. Ornithine transcarbamoylase deficiency
Transamination & Deamination
1. Transamination is the process of:
A. Removal of amino group as ammonia
B. Transfer of amino group from one amino acid to a keto acid
C. Formation of urea
D. Protein synthesis
2. Which enzyme catalyzes transamination reactions?
A. Deaminase
B. Transaminase (Aminotransferase)
C. Urease
D. Peptidase
3. The coenzyme required for transaminase activity is:
A. NAD+
B. FAD
C. Pyridoxal phosphate (Vitamin B6)
D. Biotin
4. Deamination primarily involves:
A. Transfer of amino group
B. Removal of amino group as ammonia
C. Formation of peptide bond
D. Transfer of phosphate group
5. Oxidative deamination mainly occurs in:
A. Liver mitochondria
B. Cytosol of muscle cells
C. Blood plasma
D. Kidney cortex
6. The most common amino acid undergoing transamination is:
A. Glycine
B. Glutamate
C. Alanine
D. Lysine
7. Glutamate dehydrogenase catalyzes:
A. Transamination
B. Oxidative deamination of glutamate
C. Urea synthesis
D. Protein breakdown
8. The amino group removed during deamination enters the urea cycle as:
A. Ammonia (NH3)
B. Nitrite (NO2-)
C. Nitrate (NO3-)
D. Urea directly
9. Which of the following amino acids does NOT undergo transamination?
A. Alanine
B. Glutamate
C. Lysine
D. Aspartate
10. Transamination is important for:
A. Synthesizing new amino acids
B. Breaking down carbohydrates
C. DNA replication
D. Fat metabolism
✅ Answer Key
-
B. Transfer of amino group from one amino acid to a keto acid
-
B. Transaminase (Aminotransferase)
-
C. Pyridoxal phosphate (Vitamin B6)
-
B. Removal of amino group as ammonia
-
A. Liver mitochondria
-
B. Glutamate
-
B. Oxidative deamination of glutamate
-
A. Ammonia (NH3)
-
C. Lysine
-
A. Synthesizing new amino acids
Transmethylation & Decarboxylation
1. Transmethylation is the process of:
A. Removal of a carboxyl group
B. Transfer of a methyl group from one molecule to another
C. Removal of an amino group
D. Formation of a peptide bond
2. The common methyl donor in transmethylation reactions is:
A. S-adenosylmethionine (SAM)
B. Folic acid
C. Vitamin B12
D. Pyridoxal phosphate
3. Which vitamin is essential for methylation reactions?
A. Vitamin C
B. Vitamin B6
C. Vitamin B12
D. Vitamin K
4. Decarboxylation involves the removal of:
A. An amino group
B. A carboxyl group as CO2
C. A phosphate group
D. A methyl group
5. Decarboxylation of amino acids produces:
A. Ammonia
B. Amines and CO2
C. Urea
D. Peptides
6. Which enzyme catalyzes the decarboxylation of amino acids?
A. Decarboxylase
B. Transaminase
C. Deaminase
D. Kinase
7. Which of the following is a product of decarboxylation of histidine?
A. Serotonin
B. Histamine
C. Dopamine
D. Acetylcholine
8. The coenzyme required for amino acid decarboxylation is:
A. NAD+
B. Pyridoxal phosphate (Vitamin B6)
C. Biotin
D. FAD
9. Which of the following neurotransmitters is formed by decarboxylation of L-DOPA?
A. Serotonin
B. Dopamine
C. Norepinephrine
D. GABA
10. Transmethylation reactions are important for:
A. DNA methylation and gene regulation
B. Energy production
C. Protein degradation
D. Fatty acid synthesis
✅ Answer Key
-
B. Transfer of a methyl group from one molecule to another
-
A. S-adenosylmethionine (SAM)
-
C. Vitamin B12
-
B. A carboxyl group as CO2
-
B. Amines and CO2
-
A. Decarboxylase
-
B. Histamine
-
B. Pyridoxal phosphate (Vitamin B6)
-
B. Dopamine
-
A. DNA methylation and gene regulation
Products of Glycine, Tyrosine & Tryptophan
1. Glycine is a precursor for the synthesis of:
A. Creatine
B. Dopamine
C. Serotonin
D. Thyroxine
2. Which molecule is formed from glycine and is a major component of heme?
A. Porphyrin
B. Melanin
C. Adrenaline
D. Histamine
3. Tyrosine is a precursor for the synthesis of:
A. Melanin
B. Thyroxine
C. Dopamine
D. All of the above
4. The neurotransmitter dopamine is synthesized from:
A. Glycine
B. Tryptophan
C. Tyrosine
D. Histidine
5. Which hormone is synthesized from tyrosine in the thyroid gland?
A. Cortisol
B. Thyroxine (T4)
C. Insulin
D. Glucagon
6. Tryptophan is the precursor of:
A. Serotonin
B. Melanin
C. Adrenaline
D. Thyroxine
7. Which vitamin is required for the conversion of tryptophan to serotonin?
A. Vitamin B1
B. Vitamin B6
C. Vitamin C
D. Vitamin D
8. Melanin is synthesized from which amino acid?
A. Glycine
B. Tyrosine
C. Tryptophan
D. Glutamate
9. A deficiency in which amino acid could affect serotonin production?
A. Glycine
B. Tyrosine
C. Tryptophan
D. Alanine
10. Creatine, important for muscle energy storage, is synthesized from:
A. Glycine
B. Tyrosine
C. Tryptophan
D. Phenylalanine
✅ Answer Key
-
A. Creatine
-
A. Porphyrin
-
D. All of the above
-
C. Tyrosine
-
B. Thyroxine (T4)
-
A. Serotonin
-
B. Vitamin B6
-
B. Tyrosine
-
C. Tryptophan
-
A. Glycine
Phenylketonuria and Alkaptonuria
1. Phenylketonuria is caused by a deficiency of which enzyme?
A. Tyrosinase
B. Phenylalanine hydroxylase
C. Homogentisate oxidase
D. Fumarase
2. The primary amino acid that accumulates in phenylketonuria is:
A. Tyrosine
B. Phenylalanine
C. Homogentisic acid
D. Tryptophan
3. One characteristic clinical feature of untreated PKU is:
A. Blue-black pigmentation of cartilage
B. Severe mental retardation
C. Hyperpigmentation
D. Hyperglycemia
4. The diagnostic test for PKU in newborns is:
A. Guthrie test
B. Blood glucose test
C. Urine ketone test
D. Serum bilirubin test
5. Alkaptonuria is due to deficiency of which enzyme?
A. Phenylalanine hydroxylase
B. Homogentisate oxidase
C. Tyrosinase
D. Dopachrome tautomerase
6. The accumulation of which substance causes dark urine in alkaptonuria?
A. Phenylalanine
B. Homogentisic acid
C. Tyrosine
D. Melanin
7. Which of the following is a clinical feature of alkaptonuria?
A. Intellectual disability
B. Blue-black pigmentation of connective tissue (ochronosis)
C. Hypoglycemia
D. Jaundice
8. The pigment responsible for ochronosis in alkaptonuria is derived from:
A. Melanin
B. Homogentisic acid polymer
C. Bilirubin
D. Hemoglobin
9. The inheritance pattern of both phenylketonuria and alkaptonuria is:
A. Autosomal dominant
B. X-linked recessive
C. Autosomal recessive
D. Mitochondrial
10. Dietary management of PKU includes:
A. High protein diet
B. Restriction of phenylalanine
C. Vitamin B12 supplementation
D. High tyrosine intake
✅ Answer Key
-
B. Phenylalanine hydroxylase
-
B. Phenylalanine
-
B. Severe mental retardation
-
A. Guthrie test
-
B. Homogentisate oxidase
-
B. Homogentisic acid
-
B. Blue-black pigmentation of connective tissue (ochronosis)
-
B. Homogentisic acid polymer
-
C. Autosomal recessive
-
B. Restriction of phenylalanine
Branched-Chain Ketoaciduria & Cystinuria
1. Branched-Chain Ketoaciduria is also known as:
A. Phenylketonuria
B. Maple Syrup Urine Disease (MSUD)
C. Alkaptonuria
D. Cystinuria
2. The defective enzyme complex in Maple Syrup Urine Disease is:
A. Branched-chain α-ketoacid dehydrogenase
B. Phenylalanine hydroxylase
C. Homogentisate oxidase
D. Cystathionine β-synthase
3. Accumulation of which amino acids occurs in MSUD?
A. Phenylalanine, Tyrosine
B. Leucine, Isoleucine, Valine
C. Glycine, Serine
D. Cysteine, Methionine
4. The characteristic odor of urine in MSUD is:
A. Musty
B. Sweaty feet / Maple syrup-like
C. Rotten fish
D. Mousy
5. Cystinuria is caused by defective renal tubular reabsorption of:
A. Branched-chain amino acids
B. Sulfur-containing amino acids like cystine
C. Aromatic amino acids
D. Basic amino acids only
6. Which amino acid forms crystals and stones in cystinuria?
A. Methionine
B. Cystine
C. Leucine
D. Phenylalanine
7. The inheritance pattern of cystinuria is:
A. Autosomal dominant
B. Autosomal recessive
C. X-linked recessive
D. Mitochondrial
8. The treatment for cystinuria involves:
A. Restriction of cystine in diet
B. Alkalinization of urine to increase cystine solubility
C. High protein diet
D. Low sodium diet only
9. Which of the following is NOT a clinical feature of MSUD?
A. Mental retardation
B. Seizures
C. Blue-black pigmentation of cartilage
D. Vomiting and lethargy
10. Diagnosis of cystinuria is confirmed by the presence of:
A. Sulfite crystals in urine
B. Cystine crystals in urine
C. Ketone bodies in urine
D. Hematuria only
✅ Answer Key
-
B. Maple Syrup Urine Disease (MSUD)
-
A. Branched-chain α-ketoacid dehydrogenase
-
B. Leucine, Isoleucine, Valine
-
B. Sweaty feet / Maple syrup-like
-
B. Sulfur-containing amino acids like cystine
-
B. Cystine
-
B. Autosomal recessive
-
B. Alkalinization of urine to increase cystine solubility
-
C. Blue-black pigmentation of cartilage
-
B. Cystine crystals in urine
Revision Questions
1. All amino acids are optically active except:
A. Glycine
B. Alanine
C. Leucine
D. Serine
2. Which of the following amino acids contains a sulfur group?
A. Lysine
B. Methionine
C. Glutamine
D. Phenylalanine
3. A patient presents with mousy odor of urine. The likely diagnosis is:
A. Alkaptonuria
B. Phenylketonuria
C. Maple syrup urine disease
D. Homocystinuria
4. Transamination reactions require which coenzyme?
A. FAD
B. NAD+
C. Biotin
D. Pyridoxal phosphate (Vitamin B6)
5. Which amino acid acts as a precursor for serotonin?
A. Tyrosine
B. Phenylalanine
C. Tryptophan
D. Histidine
6. The amino acid that disrupts alpha-helix structure in proteins is:
A. Alanine
B. Glycine
C. Proline
D. Glutamate
7. Which amino acid is both glucogenic and ketogenic?
A. Leucine
B. Lysine
C. Isoleucine
D. Valine
8. In urea cycle, ammonia is derived from:
A. Glutamine and alanine
B. Glutamate and aspartate
C. Glutamate and free NH₃
D. Ornithine and NH₃
9. Which enzyme is deficient in alkaptonuria?
A. Homogentisate oxidase
B. Tyrosinase
C. Phenylalanine hydroxylase
D. DOPA decarboxylase
10. Maple syrup urine disease is due to defect in metabolism of:
A. Aromatic amino acids
B. Sulfur-containing amino acids
C. Branched-chain amino acids
D. Basic amino acids
11. The positive nitrogen balance is seen in:
A. Starvation
B. Pregnancy
C. Cachexia
D. Liver failure
12. Which protein has a triple helical structure?
A. Keratin
B. Collagen
C. Elastin
D. Myosin
13. Which amino acid is a precursor of nitric oxide (NO)?
A. Citrulline
B. Glutamate
C. Arginine
D. Ornithine
14. The enzyme deficient in homocystinuria is:
A. Homogentisate oxidase
B. Cystathionine β-synthase
C. Tyrosinase
D. Glutamate dehydrogenase
15. Tyrosine is a precursor for all except:
A. Dopamine
B. Melanin
C. Thyroxine
D. Serotonin
16. Which is a semi-essential amino acid?
A. Arginine
B. Leucine
C. Tryptophan
D. Threonine
17. Which is a sulfur-containing amino acid?
A. Serine
B. Cysteine
C. Valine
D. Asparagine
18. Protein digestion begins in:
A. Mouth
B. Stomach
C. Duodenum
D. Ileum
19. Which plasma protein has the highest concentration?
A. Transferrin
B. Albumin
C. Globulin
D. Fibrinogen
20. Which amino acid carries ammonia from muscle to liver?
A. Glutamate
B. Glutamine
C. Alanine
D. Aspartate
21. The key enzyme in the urea cycle is:
A. Carbamoyl phosphate synthetase I
B. Ornithine transcarbamylase
C. Argininosuccinate synthetase
D. Arginase
22. Which bond stabilizes secondary structure of proteins?
A. Hydrogen bonds
B. Disulfide bonds
C. Peptide bonds
D. Ionic bonds
23. Which amino acid is ketogenic only?
A. Isoleucine
B. Tyrosine
C. Leucine
D. Phenylalanine
24. In electrophoresis at pH 8.6, albumin migrates:
A. Toward cathode
B. Toward anode
C. Remains at origin
D. Moves slowly
25. What is the end product of phenylalanine metabolism?
A. Tyrosine
B. Fumarate and acetoacetate
C. Pyruvate
D. Succinyl-CoA
26. Basic amino acids include all except:
A. Arginine
B. Lysine
C. Histidine
D. Glutamine
27. Most important buffering amino acid in plasma proteins:
A. Glutamate
B. Histidine
C. Glycine
D. Cysteine
28. Which amino acid forms disulfide bonds?
A. Serine
B. Alanine
C. Cysteine
D. Methionine
29. Amino acid with an imino group is:
A. Glycine
B. Proline
C. Alanine
D. Tryptophan
30. Proteins are first digested by:
A. Trypsin
B. Pepsin
C. Aminopeptidase
D. Carboxypeptidase
✅ Answer Key
| Q | Ans | Q | Ans | Q | Ans | Q | Ans |
|---|---|---|---|---|---|---|---|
| 1 | A | 9 | A | 17 | B | 25 | B |
| 2 | B | 10 | C | 18 | B | 26 | D |
| 3 | B | 11 | B | 19 | B | 27 | B |
| 4 | D | 12 | B | 20 | C | 28 | C |
| 5 | C | 13 | C | 21 | A | 29 | B |
| 6 | C | 14 | B | 22 | A | 30 | B |
| 7 | C | 15 | D | 23 | C | ||
| 8 | C | 16 | A | 24 | B |
Case Based and Analytical MCQs
Q1.
A newborn presents with a musty body odor, developmental delay, and seizures. Urine analysis reveals phenylpyruvate. Which enzyme is most likely deficient?
A. Phenylalanine hydroxylase
B. Tyrosinase
C. Homogentisate oxidase
D. DOPA decarboxylase
Q2.
A child with alkaptonuria passes dark-colored urine and has ochronosis. The deficiency is in the enzyme:
A. Homogentisate oxidase
B. Fumarylacetoacetate hydrolase
C. Tyrosinase
D. Phenylalanine hydroxylase
Q3.
A patient has maple syrup odor in urine, lethargy, and poor feeding. The metabolic block is in:
A. Homocysteine metabolism
B. Branched-chain amino acid degradation
C. Phenylalanine degradation
D. Tryptophan metabolism
Q4.
A 5-year-old boy has lens dislocation, tall stature, and a positive urinary cyanide-nitroprusside test. What is the likely amino acid abnormality?
A. Glycine
B. Methionine
C. Homocysteine
D. Tryptophan
Q5.
A patient presents with niacin deficiency symptoms and diarrhea. He is diagnosed with Hartnup disease. Which amino acid transport is defective?
A. Tyrosine
B. Tryptophan
C. Phenylalanine
D. Histidine
Q6.
Which amino acid is both ketogenic and glucogenic?
A. Lysine
B. Leucine
C. Tyrosine
D. Arginine
Q7.
Which amino acid is most important in ammonia transport from peripheral tissues to the liver?
A. Alanine
B. Aspartate
C. Glutamine
D. Glycine
Q8.
In protein structure, hydrogen bonding between NH and CO groups in the backbone is characteristic of:
A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure
Q9.
In a patient with a deficiency of carbamoyl phosphate synthetase I, what is the major consequence?
A. Hyperammonemia
B. Hypoglycemia
C. Hypouricemia
D. Ketoacidosis
Q10.
A liver biopsy shows microvesicular steatosis and low urea levels. Ammonia is elevated. Which metabolic cycle is impaired?
A. Glycolysis
B. TCA cycle
C. Urea cycle
D. Cori cycle
Q11.
Which amino acid acts as a precursor for serotonin?
A. Tyrosine
B. Phenylalanine
C. Histidine
D. Tryptophan
Q12.
Which of the following protein structures is disrupted by denaturation?
A. Primary only
B. Primary and secondary
C. Secondary and tertiary
D. Quaternary only
Q13.
A child presents with mental retardation and photosensitivity. Urinary porphobilinogen and ALA are elevated. What is the most likely diagnosis?
A. Tyrosinemia
B. Homocystinuria
C. Acute intermittent porphyria
D. Alkaptonuria
Q14.
A positive ninhydrin test indicates the presence of:
A. Lipids
B. Reducing sugars
C. Free amino acids
D. Nucleic acids
Q15.
Which protein is most abundant in plasma and maintains oncotic pressure?
A. Fibrinogen
B. Albumin
C. Transferrin
D. Globulin
Q16.
In electrophoresis at alkaline pH, which plasma protein migrates the fastest toward the anode?
A. Albumin
B. Gamma globulin
C. Beta globulin
D. Alpha-1 globulin
Q17.
Cystinuria results from a defect in renal transport of:
A. Neutral amino acids
B. Basic amino acids
C. Aromatic amino acids
D. Cystine and dibasic amino acids
Q18.
Which amino acid is a precursor for melanin?
A. Tryptophan
B. Tyrosine
C. Phenylalanine
D. Histidine
Q19.
Which enzyme catalyzes the conversion of glutamate to α-ketoglutarate with the release of ammonia?
A. Transaminase
B. Glutamate dehydrogenase
C. Glutaminase
D. Carbamoyl phosphate synthetase II
Q20.
The collagen triple helix structure is stabilized by the presence of:
A. Tryptophan
B. Tyrosine
C. Hydroxyproline
D. Methionine
✅ Answer Key
-
A. Phenylalanine hydroxylase
-
A. Homogentisate oxidase
-
B. Branched-chain amino acid degradation
-
C. Homocysteine
-
B. Tryptophan
-
C. Tyrosine
-
C. Glutamine
-
B. Secondary structure
-
A. Hyperammonemia
-
C. Urea cycle
-
D. Tryptophan
-
C. Secondary and tertiary
-
C. Acute intermittent porphyria
-
C. Free amino acids
-
B. Albumin
-
A. Albumin
-
D. Cystine and dibasic amino acids
-
B. Tyrosine
-
B. Glutamate dehydrogenase
-
C. Hydroxyproline