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IVRI Model Paper
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 proteinâs 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 âmolten globuleâ 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 âreservoirâ 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.
