PROTEINS & AMINO ACIDS

1. The peptide bond:

a) Links two amino acids
b) Links two nucleotides
c) Is weaker than the hydrogen bond
d) Is broken by mild heating
e) Is a non-covalent bond

2. The most important function of proteins in our body is:

a) Emulsification
b) Thermal insulation
c) Storage
d) Catalysis
e) Energy production

3. Aliphatic non polar amino acids are exemplified by:

a) Isoleucine and Serine
b) Histidine and Alanine
c) Cysteine and Valine
d) Aspartate and Glycine
e) Valine and Isoleucine

4. The following amino acids contain two carboxylic groups:

a) D and E
b) Q and Y
c) A and K
d) C and M
e) H and R

5. Positively charged amino acids are:

a) P and R
b) L and T
c) K and R
d) H and M
e) N and F

6. The primary structure of proteins:

a) Refers to the sequence of amino acids in the polypeptide chain
b) Refers to the helical structure of the protein
c) Describes the beta-pleated sheets
d) Is maintained by hydrogen bonds
e) Is maintained by hydrophobic interactions
7. Denaturation of a protein involves loss of its:
a) Primary structure
b) Secondary & Tertiary structure
c) Primary & Tertiary structure
d) Primary & Quaternary structure
e) Amino acids

8. The alpha helix in a protein:

a) Refers to its tertiary structure
b) Is not affected by amino acid sequence
c) Is stabilized by covalent bonds
d) Refers to its secondary structure
e) Is the quaternary structure

9. Glycoproteins contain sugar residues covalently bonded to:

a) Lysine
b) Methionine
c) Leucine
d) Asparagine
e) Cysteine

10. The following amino acids contain two carboxylic groups:

a) Aspartate and Glutamate
b) Asparagines and Glutamine
c) Glutamine and Aspartate
d) Proline and Glutamate
e) Glycine and Methionine

11. Positively charged amino acids are:

a) Valine and Arginine
b) Leucine and Lysine
c) Lysine and Arginine
d) Histidine and Cystine
e) Arginine and Glutamine

12. Sulphur containing amino acids:

a) Are non-polar
b) Include cysteine and methionine
c) Are involved in disulphide bridges
d) Are involved in methyl group donation
e) Are non essential amino acids

13. The alpha helix in a protein:

a) Describes the secondary structure
b) Is stabilized by peptide bonds
c) Stabalized by hydrogen bonds between NH and CO main chain groups
d) Is the basis for quaternary structure formation
e) Dictates its tertiary structure
14. The following are classified as acidic amino acids:
a) H and R
b) D and E
c) E and Y
d) A and K
e) C and D

15. Albumin is an important carrier of:

a) Fatty acids and glucose
b) Hyroxine and glycerol
c) Bilirubin and calcium
d) Ammonia and urea
e) Lactate and bilirubin

16. Hemoglobin and myoglobin have the same:

a) Oxygen affinity
b) Primary structure
c) Quaternary structure
d) Prosthetic group
e) Molecular weight

17. The branched chain amino acids:

a) Are isoleucine and serine
b) Include histidine and valine
c) Undergo transamination and oxidative decarboxylation by similar reactions
d) Are valine, aspartate and glycine
e) Are serine, leucine and isoleucine

18. Hemoglobin and myoglobin:

a) Have the same oxygen affinity
b) Are found in red blood cells
c) Are multimeric protein structures
d) Contain heme
e) Have the same molecular weight

19. Albumin is an important carrier of:

a) Fatty acids and bilirubin
b) Thyroxine and insulin
c) Bilirubin and retinol
d) Calcium and zinc
e) Iron and copper

20. Hemoglobin and cytochromes:

a) Contain Fe3+ as part of the active site
b) Contain heme as prosthetic group
c) Transports oxygen
d) Have similar affinity for oxygen
e) Are found in the mitochondria
21. The alpha helix in a protein:
a) Refers to its tertiary structure
b) Is not affected by the amino acid sequence
c) Is stabilized by covalent bonds
d) Refers to its secondary structure
e) Is the quaternary structure

22. Properties of the peptide bond include:

a) It is a covalent double bond
b) It links to alpha amino acids covalently
c) It is weaker than the hydrogen bond
d) It can be broken by mild heating
e) None of the above

23. Among the important functions of proteins in our body are:

a) Emulsification and buffering
b) Thermal insulation and energy production
c) Storage of energy and transport
d) Catalysis and hormonal function
e) Buffering and hydrophobocity

24. Negatively charged amino acids:

a) Are serine and glutamate
b) Include glutamine and asparagene
c) Are necessary for protein-protein interactions
d) Are not found in membrane bound proteins
e) Form disulphide bridges

25. Sulphur containing amino acids:

a) Are cysteine and methionine
b) Are non-essential amino acids
c) Can be synthesized from serine
d) Are always found at the carboxy terminal of the polypeptide chain
e) All of the above are correct

26. Albumin is:

a) Synthesized in the liver
b) Water-soluble protein
c) A carrier of bilirubin and calcium
d) Decreased in blood and in protein calorie malnutrition
e) All of the above

27. Hemoglobin S:
a) Results from insertion of a nucleotide
b) Results from substitution mutation
c) Is incompatible with life
d) The deficiency manifest in all children of carrier parents
e) Has the same affinity for oxygen as hemoglobin F
28. All of the following are considered "weak interactions" in proteins except:
a) Van der Waals force
b) Hydrogen bonds
c) Ionic bonds
d) Peptide bonds
e) Hydrophobic interactions

29. Hemoglobin:
a) Has a quaternary structure
b) Contains porphyrin ring
c) Contribute to pH maintenance in blood
d) Affinity towards oxygen increases with cooperativity
e) All of the above is correct

30. Globular proteins:

a) Are structural proteins
b) Include peptide hormones
c) Are always found in the plasma membrane
d) Are relatively water insoluble
e) Are always glycosylated

31. The following are peptides:

a) Glutathione and vasopressin
b) Gramicidin and tyrosine
c) Vasopressin and epinephrine
d) Ceramide and endorfens
e) Guanosine and insulin

32. Glycoproteins contain sugar residues covalently boded to:

a) Threonine and serine
b) Leucine and arginine
c) Asparagine and glycine
d) Cysteine and histidine
e) Lysine and methionine

33. The following is true about amino acids:

a) Cysteine and serine are polar uncharged
b) Methionine can form a cross link between peptides
c) Histidine and glutamic acid are negatively charged
d) Glycine has D and L isomers
e) Tyrosine is a basic amino acid

34. Enzymes involved in protein digestion are mainly produced by:

a) Stomach
b) Duodenum
c) Jejunum
d) Ileum
e) Pancreas
35. Glycoproteins contain sugar residues covalently boded to:
a) Lysine
b) Threonine
c) Leucine
d) Asparagine
e) Cysteine

36. The following amino acids have nonpolar side chains:

a) Valine and serine
b) Methionine and leucine
c) Arginine and alanine
d) Glycine and asparagine
e) Isoleucine and valine

37. The following is true about amino acids:

a) Ornithine is alpha amino acid
b) Glycine has two carbon atoms
c) Proline is an imino acid
d) All of the above are true
e) Valine is an aromatic amino acid

38. Which of the following amino acids is most likely to be found in the
transmembrane region of a protein?
a) Lysine
b) Arginine
c) Leucine
d) Aspartate
e) Glutamate

39. Which of the following amino acids are found in the cell but not in protein?
a) Citrulline and ornithine
b) Alanine and phosphotyrosine
c) Citrulline and cysteine
d) Gamma carboxyglutamate and hydroxylysine
e) Phosphoserine and phosphothreonine

40. The sequence of amino acids are found in the cell but not in protein?
a) Glycine-cysteine-glutamate
b) Cysteine-glycine-glutamate
c) Glycine-glutamate-cysteine
d) Glutamate-cysteine-glycine
e) Glutamate-glycine-cysteine

41. The following are peptides:

a) Glutathione and methionine
b) Gramicidin S and vaspressin
c) Vassopressin and sphingosine
d) Ceramide and insulin
e) Arginine and adrenaline
42. Properties of the peptide bond include:
a) It is a covalent double bond
b) It links three alpha-amino acids covalently
c) It is stronger than the hydrogen bond
d) It can be broken by mild heating
e) None of the above

43. Alpha helix:

a) Is stabilized by covalent bonds
b) Has 3.6 amino acid residues per turn
c) Proline favors its formation
d) Denotes secondary structure of a protein
e) Can be found in a tripeptide

44. Denaturation of a protein:

a) Disrupts the primary structure of the protein
b) Alters the secondary and tertiary structures of the protein
c) Breaks all covalent bonds in the protein
d) Has no effect on the biological activity
e) Removes disulphide bridges

45. The amino acids with positively charged side chains include:
a) Arginine and serine
b) Glutamine and alanine
c) Glutamate and proline
d) Glutamine and tyrosine
e) Arginine and lysine

46. In the polypeptide chain, the peptide bond:

a) Is formed by the alpha carboxylic group of one amino acid and the alpha
amino group of the next amino acid
b) Is rigid
c) Components are planner
d) Is stronger than a single covalent bond
e) All of the above is correct

47. The tertiary structure of a protein is:

a) Its three dimensional structure
b) The relationship between different subunits
c) Not lost by denaturation
d) Stabalized by peptide bonds only
e) Not relevant to its function

48. The major functions of proteins in the human body include:

a) Storage of genetic information
b) Immunity and locomotion
c) Buffering and transport
d) Catalysis and signalling
e) B, C and D are correct
49. Non standard amino acids in protein structure include:
a) Ornithine
b) Citrulline
c) Hydroxyproline
d) Serine
e) Glycine

50. The pancreatic enzyme not involved in protein digestion is:

a) Carboxypeptidase
b) Trypsin
c) Lipase
d) Clastase
e) Chymotrypsin