Analytical 10
Analytical 10
Analytical 10
1 At neutral pH(pH = 7) :
at
(a) isoleucine (b) valine (c) methionine (d) arginine
lat
3 Which of the following amino acids contain(s) a sulfur atom?
6 Which of the following amino acids has (have) two chiral centers?
Arh/A
7 Which of the following best describes the order of elution of a mixture of asparagine, lysine,
and serine (from first to last) from a cation exchange column?
D/D
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Dr/Ahmed Talaat Analytical Chemistry
10 The peptide linkage between amino acids has partial double bond character. Because of this
A. There is free rotation around the peptide bond.
B. The carbonyl and amino groups always reside on the same side of the bond.
11 The type of bond holding the amino acid units together in a dipeptide molecule is called:
(a) a glycosidic bond (b) an ester bond (c) a peptide bond (d) a protein bond
at
12 All amino acids have the following pair of functional groups:
lat
(a) amine and an ester (b) carboxylic acid and an amine
13 Two amino acid molecules combine to form a dipeptide molecule. The reaction that occurs
is:
(a) made from non-essential amino acids (b) obtained by eating the correct food
15 When complex biomolecules such as proteins are unfolded and disordered from their biologically
Arh/A
16 The arrangement of the two alpha and two beta polypeptide chains in hemoglobin is an
example of the ............structure of a protein.
17 Which of the following noncovalent interactions are NOT important in protein structure?
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(a)The forming of hydrophobic bonds maximizes the interaction of nonpolar residues with water.
(b)They form because nonpolar side chains of amino acids and other nonpolar solutes prefer to
cluster in a nonpolar environment.
(d)They form because nonpolar side chains prefer not to intercalate in a polar solvent such as
water.
at
19 Which of the following statements about electrostatic interactions is false?
lat
(a)They arise either as electrostatic attractions between opposite charges or repulsions between
like charges.
(b)Electrostatic interactions between charged groups on a protein surface are often complicated
by the presence of salts.
Dr/Ahmed
20 Which of the following statements
Ta
(d)Most proteins do not have amino acids that participate in electrostatic interactions.
(d)Because they are so weak, they do not contribute much to protein stability.
(a)The side chains extend outward from the core structure of the helix.
(c)All of the carbonyl groups point in one direction along the helix axis.
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23 The term used to refer to how individual polypeptide chains of a protein Kaving two or more
chains are arranged in relation to each other is:
at
(c)two or more proteins bonded together
lat
(d)a protein and a carbohydrate bonded together
26 Which of the following types of bond is not present within or between protein molecules:
4 A/An ..................is the formation of a covalent bond between two molecules during which the
elements of water are lost.
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5 A loop is a segment of a/an ...................usually found on the protein surface, that joins two
elements of secondary structure.
7 ..................... is a procedure for the stepwise removal and identification of the N-terminal
residues of a polypeptide.
at
9 ...............is the local spatial arrangement of a polymer’s backbone atoms without regard to
the conformations of its substituent side chains.
lat
10 A stretch of polypeptide residues that fold into a globular unit with a hydrophobic core is
called a/an.....................
13
Ta
11 An ion pair is an electrostatic interaction between two ionic groups of ...................charge.
2 Free ammonia combined with glutamate to yield glutamine by the action of................
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3 Pyridoxal phosphate and its aminate form, pyridoxamine phosphate are tightly bound coenzymes
of..............
at
5 Which is the first step in the catabolism of most L-amino acids once they have reached the
lat
liver is promoted?
(b) Glutaminase
9 The first enzyme in the pathway carbamoyl phosphate synthase I, is allosterically activated
D/D
by...........
11 Nitrogen atoms of urea produced in the urea cycle are derived from...............
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(a) One molecule of urea, one molecule of ammonia, one molecule of ATP and one molecule of
fumaric acid
(b) One molecule of urea, one molecule of AMP, two molecules of ADP and one molecule of
fumaric acid
(c) One molecule of aspartic acid, one molecule of ammonia, one molecule of ATP and one molecule
of fumaric acid
at
(d) Two molecules of urea, two molecules of ammonia, one molecule of ATP and one molecule of
fumaric acid
lat
13 The carbon atom source while producing urea in the urea cycle is............
(b) Leucine
Talaat
(b) Amino
(d) Histidine
(c) Ammonia into a less toxic form (d) Ammonia into a more toxic form
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at
(c) Alpha-ketoglutarate (d) Aspartic acid
lat
25 3. Which enzyme catalyzes the reductive amination of ketoglutarate?
(c) Alpha-ketoglutarate
Ta
26 Which product is formed after the degradation of glutamic acid?
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(c)Glutaminase 3. Alpha-ketoglutarate
at
32 Glutaminase is particularly important in which organ?
lat
(a) Kidney (b) Brain (c) Liver (d) Shoulder
(a) Oxaloacetate (b) Pyruvate (c) Aspartic acid (d) Glutamic acid
(a) Aspartic acid (b) Glutamic acid (c) Proline (d) All of the above
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(c)Both
(d)None
(a) Liver (b) Kidney (c) Muscle (d) All of the above
at
40 In which form, the ammonia is transported into the blood?
lat
(a) Alanine (b) Pyruvate (c) Glutamine (d) Both A and c
(c) Both
Ta
42 Which type of amino acid is used in the muscle as source of fuel?
(d) None
Dr/Ahmed Talaat
ede
43 During which condition, amino acid acts as fuel in muscle?
mhm
(a) Exercise (b) Fasting (c) During rest (d) Both A and B
(d)Both B and C
(a) Kidney (b) Brain (c) Liver (d) All of the above
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(a) Alanine (b) Pyruvate (c) Glucose (d) None of the above
at
(c)There are 3 isoenzymes of mitochondrial glutaminase
lat
(d)For the synthesis of glutamine, ammonia is required
(a) ALT
(d) None of the above
(b) AST
Dr/Ahmed Talaat
ede
(c) Pyruvate kinase (d) Pyruvate decarboxylase
mhm
53 Tyrosine is normally a nonessential amino acid, but why do individuals with a genetic defect
phenylketonuria require tyrosine in their diet for normal growth? Choose the correct answer.
D/D
(a) i) only (b) i) and ii) (c) ii) and iii) (d) i) and iv)
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54 Which one of the following amino acids is synthesized by a single step of transamination?
(a) Aspartate (b) Glutamate (c) Alanine (d) All the above
55 Amino acids are derived from the intermediates in one of the following metabolic pathways
at
(c) Glutaminase (d) Asparagine synthetase
lat
57 Which one of the following option is correct about the precursors of aromatic amino acid
i) Erythrose 4-phosphate
ii) Pyruvate
iii) Phosphoenolpyruvate
iv) Onaloacetate
Dr/Ahmed
58 Histidine is synthesized from one
Ta
(c) i) and iv)
Talaat
of the following metabolites..
(d) ii) and ii)
ede
mhm
i) Alanine
ii) Valine
iii) Isoleucine
D/D
iv) Leucine
(a) i) only (b) i) and ii) (c) i), ii) and iii) (d) i), ii), iii) and iv)
(a) Glycine (b) Cysteine (c) Serine (d) All the above
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62 Select one of the most appropriate enzyme target being used lymphoblastic leukemia and
acute myeloblastic leukemia
at
i) Asparaginase
lat
ii) Asparagine synthetase
iii) Glutaminas
iv) Glutamine synthetase
(a) i) only
(a) Carbohydrates
(b) i) and ii)
(c) Proteins
Dr/Ahmed Talaat
(d) i), ii), iii) and iv)
(d) Lipids
ede
(a) Glycine (b) Alanine (c) Asparagine (d) Tyrosine
mhm
(a) fatty acids (b) mineral salts (c) α-ketoglutaric acid(d) volatile acids
Arh/A
67 Which of the following amino acids is not necessary to be taken in the diet?
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(a) D-amino acids (b) L-amino acids (c) both (a) and (b) (d) none of these
at
lat
Ta
Dr/Ahmed Talaat
ede
mhm
Arh/A
D/D
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