Biology · Chemistry
Biomolecules and Enzymes
1,501 Questions
This topic focuses on biomolecules, specifically proteins, enzymes, and amino acids. It includes questions on enzyme structures, protein folding, and catalysis. These concepts are crucial for medical and biology competitive exams.
Enzyme catalysisProtein structuresAmino acid synthesisPolypeptide chainsBiomolecule properties
Biomolecules and Enzymes Questions
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Ribonuclease A
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Lysozyme
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Chymotrypsin
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Hexokinase
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Glutamine synthase
E
Correct answer
Explanation
Correct answer. Glutamine synthase is made up of twelve polypeptide chains.
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Carboxypeptidase and ATPase
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Carbonic anhydrase and phosphoglucomutase
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Carbonic anhydrase and carboxypeptidase
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ATPase and phosphoglucomutase
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Phosphoglucomutase and carboxypeptidase
C
Correct answer
Explanation
This option is correct because carboxypeptidase and carbonic anhydrase are zinc-containing enzymes.
Match the following Fe containing proteins with the corresponding function and oxidation state of Fe.
| |
|
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| Fe containing proteins |
|
|
|
Function |
|
|
Oxidation state of Fe |
|
| P. Haemoglobin |
i. Plasma O2 transport |
a. 2 |
| Q. Myoglobin |
ii. Muscle O2 storage |
b. 3 |
| R. Transferrin |
iii. Plasma Fe transport |
|
| S. Catalase |
iv. H2O2 metabolism |
|
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P - ii - a, Q - iv - b, R - i - b, S - iii - b
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P - iii - a, Q - iv - a, R - ii - b, S - i - b
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P - i - a, Q - ii - a, R - iii - b, S - iv - a
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P - ii - b, Q - iii - b, R - iv - a, S - i - a
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P - i - b, Q - iii - b, R - ii - a, S - iv - b
C
Correct answer
Explanation
This is the correct answer.
Haemoglobin is a plasma O2 transport protein. Oxidation number of Fe in haemoglobin is 2.
Myoglobin is a muscle O2 storage protein. Oxidation number of Fe in myoglobin is 2.
Transferrin is a plasma Fe transport protein. Oxidation number of Fe in transferrin is 3.
Catalase is an enzyme, which catalyses H2O2 metabolism. Oxidation number of Fe in catalase is 2.
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Enzymes are nucleic acids.
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Repeating units of proteins are peptides.
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Saccharides are the most abundant biomolecules on the Earth.
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Primary structure of proteins represents linear sequence of amino acids joined together by ester linkage.
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Glycogen is a polymer of galactose and glucose.
C
Correct answer
Explanation
This option is correct because saccharides (carbohydrates) are the most abundant biomolecules on the Earth.
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Nihydrin test is used for detection of α-amino acids.
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Denaturation leads to loss of primary and secondary structure of proteins.
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Keratin is an example of fibrous protein.
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Albumin is a globular protein.
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Isoelectric point is the pH at which no net migration of amino acid occurs under electric field.
B
Correct answer
Explanation
This option is correct because the denatured protein has the same primary structure as the original. Denaturation leads to loss of secondary, tertiary and quarternary structures of proteins.
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Haemoglobin and rhodopsin
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Zein and keratin
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Haemoglobin and casein
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Casein and keratin
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Rhodopsin and Zein
A
Correct answer
Explanation
Chromoproteins are proteins, such as hemoglobin or rhodopsin. They contain a pigmented nonprotein group, as heme, riboflavin, or retinal.
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Glucose
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Fat
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Carbohydrate
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Protein
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Vitamin
D
Correct answer
Explanation
Protein is known as the building block of life.
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Histidine
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Arginine
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Citrulline
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None of these
B
Correct answer
Explanation
Arginine is the substrate for the enzyme nitric oxide synthase, which converts it into nitric oxide and citrulline in biological systems.
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Actin
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Haemoglobin
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Myosin
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Myoglobin
C
Correct answer
Explanation
Myosin is a motor protein that exhibits properties of both fibrous proteins (due to its long tail) and globular proteins (due to its motor head domain).
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Amino group
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Carboxyl group
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Hydrocarbon side chains
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All of these
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Transferrin
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Globulins
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Antitrypsin
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Albumins
D
Correct answer
Explanation
Albumins, specifically serum albumin, are the most abundant proteins found in human blood plasma.
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β-hairpin
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Loop regions
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Twist regions
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α-loops
B
Correct answer
Explanation
Loop regions are flexible, unstructured segments of a polypeptide chain that connect secondary structural elements like alpha-helices and beta-strands.
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Tryptophan
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Proline
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Methionine
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Serine
C
Correct answer
Explanation
Methionine is a key amino acid in methyl group metabolism, as it is converted to S-adenosylmethionine (SAM), the primary methyl donor in the cell.
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They exist as heteropolymers
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They exist as homopolymers
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They exist as monomers
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None of these
A
Correct answer
Explanation
Proteins are heteropolymers because they are composed of a sequence of different amino acids linked together, rather than repeating units of the same monomer.
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Tryptophan
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Proline
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Methionine
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Serine
B
Correct answer
Explanation
Proline has a unique cyclic structure where the side chain is bonded to the nitrogen atom of the backbone, which restricts rotation and introduces a kink in the polypeptide chain.