Veterinary Biochemistry question bank-1

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Veterinary Biochemistry question bank-1


Hello vets , these are some important basic questions regarding Veterinary Biochemistry 
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Veterinary Biochemistry 



1. The network of interrelated catabolic and anabolic pathways in cells is referred to as ______________
2. A system that exchanges both energy and material with its surrounding is said to be ______________
3. ________________ is a type of weak interaction that stabilizes the native conformation of a biomolecule or supramolecular complex.
4. The monomeric subunits of ________ are ribonucleotides.
5. The stretching and breaking of bonds that occurs during the conversion of a reactant to a product creates a ____________ state.
6. ____________ is a measure of randomness.
7. Enzymes enhance the rate of chemical reactions by lowering the __________ energy that constitutes an energy barrier between reactants and products.
8. mRNA molecules with two or more attached ribosomes are called ____________
9. ______________ is a component of eukaryotic cells consisting of microtubules, actin filaments, and intermediate filaments.
10. _____________ and _______________ are the two groups of extant prokaryotes.
11. The role of _____________ is to produce large number of ribosomes needed by the cell and have DNA that contain many copies of ribosomal RNA coding genes.
12. ________________ helps in the condensation of DNA molecule.
13. ____________, _______________ and __________ are three classes of cytoskeletal proteins.
14. ________________ is a complex of RNA and protein.
15. ______________ are molecular complexes of DNA plus associated histone and nonhistone proteins.
16. _____________ are compounds having electron-deficient functional groups; they tend to bond to electron-rich sites.
17. ______________ are steroisomers that cannot be superimposed.
18. ________________ are a pair of stereoisomers that are not mirror images of each other.
19. ___________ is the energy or heat content of a system.
20. Henderson-Hasselbalch equation = ____________________.
21. The glycan portion of glycoprotein is known as a ___________ group.
22. A covalent bond between two adjacent cysteines in a polypeptide chain is a __________ bond.
23. All stereoisomers must have at least one __________ centre.
24. ________________ procedure provides information about a protein’s primary structure.
25. The whole assortment of proteins in an organism.
26. ______________ are cellular agents that assist in protein folding at elevated temperatures.
27. _____________ is stable arrangement of few secondary structures.
28. ______________ is an amino acid which can either accept protons or donate them at a pH that is close to physiological pH values.
29. _______________ interactions are thought to be the driving force behind the formation of “molten globule” during protein folding.
30. Individual amino acids in a protein is called a ____________.
31. ______________ refers to the portion of a protein that is often composed of noncontiguous amino acid sequences and is usually defined on the basis of its contribution to protein function.
32. _________ is a type of secondary protein structure that extends 0.15 nm per amino acid residue.
33. _________ is a type of secondary protein structure that extends 0.35nm per amino acid residue.
34. Disrupting the hydrophobic interactions of a single subunit protein would have the greatest effect on the ____________ structure of that protein.
35. Proteins that belong to a ___________ have related structural features though they are unrelated based on their amino acid sequences.
36. The alpha-beta subunits in hemoglobin comprise a single__________; the intact haemoglobin tetramer contains two of these.
37. The saddle conformation is a __________________ structure.
38. alpha-Keratin is referred to as a _______________ ____________ of protein subunits; haemoglobin with only four subunits is referred to as a(n) ____________
39. Beta turn is an example of ___________ structure.
40. ______________ occurs when the binding of one ligand increases or decreases the binding of additional ligands.
41. The _______________ immune system protects against bacterial infections.
42. ______________ has a hyperbolic oxygen binding curve, no quarternary structure and serves as an oxygen “reservoir” in muscle cells.
43. ______________ has a sigmoid oxygen binding curve and has a quaternary structure.
44. ______________ is also called programmed cell death.
45. The metabolic intermediate _________________ binds to haemoglobin with a stoichiometry of 1:1 and promotes the release of oxygen.
46. A helper T cell can signal nearby lymphocytes by secretion of a signal protein called ______________
47. The contribution of lactic acid in muscle tissue contributes to the _______ effect, which explains the link between lactate production and an increased release of oxygen from haemoglobin.
48. RBCs transport carbon dioxide produced by respiring tissues in two forms: as bicarbonate ions and as _____________
49. ___________ are small molecules covalently attached to large proteins in the laboratory in order to elicit an immune response.
50. _____________ is a particular molecular structure within antigen that binds an individual antibody.
51. Michaelis-Menten equation = ________________
52. kcat is known as the ________________ number. At saturating substrate concentrations kcat=Vmax/Et.
53. ______________ inhibitor alters the Km of an enzyme without altering Vmax.
54. An enzyme without a prosthetic group is called _____________.
55. The common structural motifs recognized by specific protein kinases are known as ______________ sequences.
56. _______________ is the enzyme that contains Ni2+ as a cofactor and was the first enzyme crystallized by Sumner. It enhances the rate of the reaction by ____.
57. A molecule essential to the functioning of an enzyme, but not part of the enzyme protein itself is called ____________
58. ______________ inhibitor binds only to the ES complex and does not bind to the substrate-binding site.
59. A specific, rare type of mixed inhibitor that alters Vmax without affecting Km is __________________ inhibitor.
60. ______________ of a substrate occurs when hydrogen bonds between a substrate molecule and water are replaced by noncovalent interactions between the substrate molecule and an enzyme.
61. ___________ is an allosteric enzyme whose activity is regulated by a modulator other than its substrate whereas _______________ is an allosteric enzyme whose substrate is also a modulator of activity.
62. When the K’eq=one, ∆G’°=___________
63. Inhibitors that rreversibly bind to an enzyme are known as ____________ inactivators.
64. The regulation of enzyme activity by the reversible binding of a phosphoryl group is an example of regulation by ___________ modification.
65. Allosteric enzymes__________(do/do not) follow Michaelis-Menten kinetics and some show ____________ kinetic behaviour in the velocity versus substrate concentration plot which reflects cooperativity.
66. The plot of an enzyme kinetic reaction eventually plateaus as the active site is saturated with substrate. [T or F]
67. Six membered ring form of sugars are called _____________ and five-membered ring form of sugars are called ____________
68. Lectins are proteins that bind to specific ______________
69. An isomer that differs at only one of two or more chiral centres are called _________
70. The process that interconverts isomers of pyranoses
71. __________ DNA is the dehydrated compact form of DNA.
72. _______ DNA is a structure containing polypurine tracts and mirror repeats and forms a triple helix.
73. __________ pairing or Non-Watson-Crick pairing allows the formation of triplex DNAs.
74. ____ of purine and ____ of pyrimidines is linked to C1 of ribose.
75. The increase in UV light absorption when double-stranded DNA is denatured is referred to as the ___________ effect.
76. Purine or pyrimidine base covalently bound to furanose through and ___________
77. ______________ bonds are covalent bonds tht link the individual nucleotide residues in DNA and RNA.
78. The deamination product of :
a) Cytosine = ____________
b) Guanine = _____________
c) 5-methyl cytosine =___________
d) Adenine = ___________
79. _____________ is an extremely hydrophobic isoprenoid compound that anchors sugars to cell membranes.
80. The polar head group of cholesterol is ____________ group.
81. ______________________ is a lipid seen in beeswax.
82. Lignoceric acid is a/an _____________ free fatty acid with _____ carbon atoms.
83. The fatty acid 20:4(∆5,8,11,14) is commonly called ____________ which is a precursor of ____________


Answers-
1) Metabolism
2) Open
3) non-covalent interaction
4) RNA
5) Transition
6) Entropy
7) Activation
8) Polysomes
9) Cytoskeleton
10) archaebacteria and eubacteria
11) nucleolus
12) nucleosome
13) actin/microfilament; microtubules; intermediate filaments
14) ribosome
15) chromatin
16) electrophiles
17) enantiomers
18) diasteromers
19) enthalpy
20) pH=pKa+log[proton acceptor]/[proton donor]
21) prosthetic
22) disulfide
23) chiral
24) Edman degradation
25) Proteome
26) Chaperones
27) Motif
28) Histidine
29) Hydrophobic
30) Residue
31) Domain
32) alpha helix
33) beta pleated sheet/beta conformation
34) tertiary
35) superfamily
36) protomer
37) supersecondary
38) supramolecular complex; oligomer
39) secondary
40) cooperativity
41) humoral
42) myoglobin
43) haemoglobin
44) apoptosis
45) 2,3-bisphosphoglycerate
46) Interleukin
47) Bohr
48) Carbaminohaemoglobin
49) Hapten
50) Epitope
51) Vo = Vmax + [S]/ Km + [S]
52) Turnover
53) Competitive
54) apoenzyme
55) Consensus
56) urease; 10^14
57) cofactor
58) uncompetitive
59) noncompetitive
60) desolvation
61) heterotropic/homotropic
62) zero
63) suicide
64) covalent
65) do not; sigmoid
66) T
67) pyranoses; furanoses
68) oligosaccharides
69) epimers
70) mutarotation
71) A-DNA
72) H-DNA
73) Hoogsteen
74) N9;N1
75) Hyperchromic
76) N-β-glycosidic bond
77) Phosphodiester
78) a. uracil; b. xanthine; c. thymine; d. Hypoxanthine
79) Dolichols
80) Hydroxyl
81) Triacontanylpalmitate
82) saturated/unsaturated; saturated;24
83) arachidonic acid; eicosanoids – an example: prostaglandins


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