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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Nitrilase
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Adenosine deaminase
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Arginase
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Urease
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Metalloendopeptidase
C
Correct answer
Explanation
Arginase is a manganese-containing enzyme. The reaction catalyzed by this enzyme is: arginine + H2O → ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life.
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Enzymes are regarded as the environmentally friendly solution to industrial problems.
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The arrangement of amino acids determines the enzyme's function.
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Enzymes neither live nor die.
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No two enzymes are alike.
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The two-dimensional structure of the enzyme determines the appearance of the active site.
E
Correct answer
Explanation
The three-dimensional structure of the enzyme determines the appearance of the active site. The active site accommodates the shape of the biological substrate that requires transformation. They fit like a key in a lock. This is what makes enzymes specific in their actions. Only substances of the right shape will be transformed.
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pancreatic lipase
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phospholipase D
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sterol esterase
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chymotrypsinogen
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trypsinogen
C
Correct answer
Explanation
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in bile acid biosynthesis.
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cysteine
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glycine
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glutamine
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cystine
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asparagines
A
Correct answer
Explanation
It provides resistance to our body and inhibits the growth of hair, nails etc.
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Allithiamine
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Benfotiamine
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Prosultiamine
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Sulbutiamine
D
Correct answer
Explanation
Sulbutiamine is a synthetic derivative of thiamine (vitamin B1). As a dimer of two modified thiamine molecules, it is a lipophilic compound that crosses the blood-brain barrier more readily than thiamine and increases the levels of thiamine and thiamine phosphate esters in the brain.
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Primary structure
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Secondary structure
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Tertiary structure
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Quaternary structure
C
Correct answer
Explanation
Tertiary structure is the final three-dimensional structure of a protein, which results from a large number of non-covalent interactions between amino acids.
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Alanine
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Asparagine
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Citrulline
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Creatine
A
Correct answer
Explanation
Alanine is necessary for the maintainance of proper blood glucose level from dietary protein. It stimulates lymphocyte production and may help people who have immune suppression. It also strengthens the immune system by producing antibodies.
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isoleucine
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L-arginine
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L-carnosine
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leucine
A
Correct answer
Explanation
Isoleucine is necessary for the optimal growth of infants and for maintaining nitrogen balance in adults.
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Indole
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Pyrrole
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Tryptophan
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Serotonin
C
Correct answer
Explanation
Tryptophan is one of the 20 standard amino acids, as well as an essential amino acid in the human diet. It is encoded in the standard genetic code as the codon UGG.
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L-theanine
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Lysine
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Phenylalanine
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Proline
A
Correct answer
Explanation
L-theanine reduces stress and anxiety without the tranquilizing effects found in many other calming supplements.
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Glycine
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Leucine
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Methionine
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Lysine
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None of these
C
Correct answer
Explanation
This option is correct because methionine amino acid is classified as non polar as it has a straight side chain that possesses a S-methyl thioether (i.e C-S-C bonding) at the gama-carbon. It is an essential amino acid in all metazoa. These are initiated by the polypeptide chain.
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Methionine
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Tryptophan
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Arginine
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Leucine
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Serine
C
Correct answer
Explanation
Arginine is an α-amino acid. At the level of molecular genetics, in the structure of the messenger ribonucleic acid mRNA, CGU, CGC, CGA, CGG, AGA, and AGG are the triplets of nucleotide bases or codons that code for arginine during protein synthesis.
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neurochemistry
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nuclear chemistry
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materials chemistry
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immunohistochemistry
D
Correct answer
Explanation
Immunohistochemistry or IHC refers to the process of detecting antigens (e.g., proteins) in cells of a tissue section by exploiting the principle of antibodies binding specifically to antigens in biological tissues. IHC takes its name from the roots immuno, in reference to antibodies used in the procedure, and histo, meaning tissue (compare to immunocytochemistry).
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fats
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vitamins
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sugars
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proteins
D
Correct answer
Explanation
Amino acids link together through peptide bonds to form proteins, making them the fundamental building blocks of all proteins. Fats are built from fatty acids and glycerol, vitamins are organic micronutrients, and sugars are carbohydrates - none of which are made from amino acids.
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Complement
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Antibodies
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Toxoids
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PGE2
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Proteolytic enzymes
B
Correct answer
Explanation
Antibodies may block the binding to target cell and would increase the rate of removal of toxin from the circulation by immune complex formation.