Biology ยท 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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Glycoliped
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Protein
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Micopolysaccharide
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Steroid
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Globulins
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Albumins
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Keratin
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Hormones
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Collagen
A
Correct answer
Explanation
They are immunoglobulins and provide immunity to the body.
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Thrombokinase
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Thrombin
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Prothrombin
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Fibrinogen
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Fibrin
B
Correct answer
Explanation
It is an essential enzyme for clot formation and converts soluble plasma protein fibrinigen into insoluble protein fibrin.
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Reactome and NetPath
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Reactome and MetaCyc
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Netpath and MANET
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Netpath and MetaCyc
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Reactome and MANET
A
Correct answer
Explanation
This option is correct because NetPath is a manually curated resource of human signal transduction pathways and Reactome is a navigable map of human biological pathways, ranging from metabolic processes (metabolic pathways) to hormonal signalling (signal transduction pathways).
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InterPro
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ModBase
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RefSeq
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SIMAP
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TreeFam
E
Correct answer
Explanation
TreeFam is a database of phylogenetic trees of animal genes which aims at developing a curated resource that gives reliable information about ortholog and paralog assignments and evolutionary history of various gene families.
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fibrinogen
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prothrombin
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thrombin
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fibrin
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Keratin
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Elastin
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Chondrin
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Albumin
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Collagen
C
Correct answer
Explanation
Cartilage is made up of a protein known as chondrin.
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It competes with the substrate for the catalytic site.
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It binds to a site other than the catalytic site.
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It changes the nature of the product formed.
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It changes the substrate specificity of the enzyme.
B
Correct answer
Explanation
Allosteric enzyme, upon binding an effector, changes its shape, which in turn changes its affinity towards its product. The effector never binds with the catalytic site of the enzyme.
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Tryptophan
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TYrosin
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Glutamate
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Serine
C
Correct answer
Explanation
GABA is systhesised from glutamate by the enzyme glutamic acid decarboxylase. It is an inhibitory neurotransmitter.
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pyruvic acid
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para-hydroxyphenylpyruvate
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phenylpyruvate
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hydroxypyruvate
A
Correct answer
Explanation
Alanine transaminase transfers its amino group, which forms pyruvate.
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SDS polyacrylamide gel electrophoresis
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Native gel electrophoresis
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Cation exchange chromatography
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Anion exchange chromatography
B
Correct answer
Explanation
SDS PAGE is not used in if a particular protein has to be separated in the basis of their biological activity. As there is no treatment with SDS, all the proteins will carry their own charge at the pH and will move according to their different electrophoretic mobilities.
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P only
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S only
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P, Q and S
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R and S
B
Correct answer
Explanation
Myoglobin is not an allosteric protein. Myoglobin has a hoghe affinity for oxygen than haemoglobin, so it has a hyperbolic curve.
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Substrate will bind to the active site of the enzyme with no inhibition.
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Both substrate and the inhibitor will compete for binding to the catalytic site of the enzyme.
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Substrate can never bind itself to the enzyme.
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None of the above
B
Correct answer
Explanation
As both the substrate and the inhibitor share the same binding site in the enzyme, they will compete with each other in binding. This will exert an competitive inhibition. If substarte concentration is increased to a greater level, then the inhibition will be released.
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Both cytosolic and extracellular proteins have similar amount of disulphide bonds.
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Cytosolic proteins lack disulphide bonds, whereas extracellular proteins have more disulphide bonds.
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Extracellular proteins lack disulphide bonds, whereas cytosolic proteins have more disulphide bonds.
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None of these
B
Correct answer
Explanation
The cytosol is a reducing environment whereas the extracellular milieu is an oxidising environment. Disulphide bonds are formed as a result of oxidation of thiol group and it requires an oxidising environment.
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it has more efficient polymerse activity
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it has proof reading activity
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both 1 and 2
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none of these
B
Correct answer
Explanation
Pfu polymerase has proof reading activity, so if there is any mispaired binding, it will repair this base pairing so that there will be no mispairing. Proof reading activity is absent in Taq polymerase, so it cannot repair any mispairing.