In β-pleated sheet structures neighbouring

  1. Home

- Online Exam Test Papers | - MCQs[multiple choice questions and answers ] | - Mock Test Papers | - Practice Papers | - Sample Test Papers |

Question:
 
In β-pleated sheet structures neighbouring

1.chains lie in a flat plane

2.neighboring residues are hydrogen bonded

3. neighboring chains are connected by a-helices

4.neighboring chains are hydrogen bonded

Posted Date:-2021-03-07 12:01:26

More MCQS Questions and answers

  1. Disulfide bonds most often stabilize the native structure of
  2. How is the enzyme COX-1 important in human health?
  3. If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?
  4. If the F and Y angles of each peptide unit in a protein are known, which of the following may also be determined?
  5. In β-pleated sheet structures neighbouring
  6. Which of the following forces is the most favorable for protein folding?
  7. In an SDS-PAGE
  8. In isoelectric focusing, proteins are separated on the basis of their
  9. In the enzyme-catalyzed reaction shown below, what will be the effect on substances A, B, C, and D of inactivating the enzyme labeled E2? A ---(E1)---> B ---(E2)---> C ---(E3)--->
  10. The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin to produce
  11. A molecule that can be covalently linked to a non-immunogenic antigen to make it an immunogen is called a (n)
  12. An oil drop with a polar coat is a metaphor referring to the three dimensional structure of
  13. Antigen, when injected in the body activates its specific lymphocytes in the
  14. At the midpoint of a temperature transition curve,
  15. Attractive Vander Waals forces occur between
  16. Before they can react, many molecules need to be destabilized. This state is typically achieved through
  17. Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of
  18. Common feature in all serine proteases is a
  19. Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in
  20. Enzyme-driven metabolic pathways can be made more efficient by
  21. For specific antigen recognition by T cells,
  22. For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that
  23. Heme is the binding pocket of myoglobin and hemoglobin and is composed of
  24. Hemoglobin has quaternary structure and is made up of
  25. In a gel filtration column
  26. In a native PAGE, proteins are separated on the basis of
  27. In deoxy hemoglobin (Hb), the Fe (II) is coordinated to
  28. In SDS-PAGE, the protein sample is first
  29. In the β-pleated sheet
  30. The molecular formula for glycine is C2H5O2N. What would be the molecular formula for a linear oligomer made by linking ten glycine molecules together by condensation synthesis?
  31. Peptides in the fully extended chain conformation
  32. Proteins are separated in an SDS-PAGE experiment on the basis of their
  33. Proteins can be visualized directly in gels by
  34. Secondary structure in protein refers to
  35. Since ΔG° = -RTlnK
  36. The cleavage specificity of trypsin and chymotrypsin depend in part on the
  37. The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues
  38. The different orders of protein structure are determined by all of the following bond types except
  39. The E.coli pyruvic acid dehydrogenase complex is reported to
  40. The heme is held in place by a bond between
  41. The major element of secondary structure in myoglobin and hemoglobin is
  42. The nature of peptide bond can be best explained as
  43. The nucleophile in serine proteases is
  44. The oxygen binding curves of hemoglobin and myoglobin
  45. The oxygen in hemoglobin and myoglobin is bound to
  46. The peptide bond in proteins is
  47. The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce:
  48. The proteolysis rate enhancement by chymotrypsin (~1010 folds) corresponds to a reduction in activation energy of about
  49. The Ramachandran Plot illustrates the fact that
  50. The resonance structures that can be drawn for the peptide bond indicate that the peptide bond
  51. The role of Asp 102 and His 57 during trypsin catalysis is to
  52. The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by
  53. Tryprotophan synthetase of E.coli, a typical bifunctional oligomeric enzyme consist of
  54. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein
  55. What is the effect of a decrease in pH on hemoglobin oxygen affinity?
  56. What is the proportion of glycine residues in collagenous regions?
  57. What is the specificity of the Clostripain protease?
  58. What was the first protein whose complete tertiary structure was determined?
  59. Which hemoglobin chain replaces the beta chain in embryonic hemoglobulin?
  60. Which of the common features are shared between serine and aspartate proteases?
  61. Which of the following (s) is/are serine proteases?
  62. Which of the following forces is the most unfavorable for protein folding?
  63. Which of the following is an example of tertiary structure in a protein?
  64. Which of the following is false statement with regard to comparison between Serine and HIV proteases?
  65. Which of the following is the most correct?
  66. Which of the following statement is incorrect?
  67. Which of the following statements about enzymes or their function is true?
  68. Which of the following statements is incorrect?
  69. Which of the three subunits of the G proteins binds GDP and GTP?
Search
R4R Team
R4Rin Top Tutorials are Core Java,Hibernate ,Spring,Sturts.The content on R4R.in website is done by expert team not only with the help of books but along with the strong professional knowledge in all context like coding,designing, marketing,etc!