
biomolecules 2
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•
Chemistry
•
12th Grade
•
Easy
Medium Verbatim
Used 2+ times
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23 Slides • 34 Questions
1
Biomolecules
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3
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6
7
Multiple Choice
What are the end products of Starch Hydrolysis?
Phenylpyruvic acid, ammonia and water
Iodine and water
Disaccharides and monosaccharides
Ammonia and nitrate gas
8
Multiple Choice
What enzyme catalyzes Starch Hydrolysis?
Amylase
Phenylalanine deaminase
Nitrate reductase
Nitrite reductase
9
Multiple Choice
On oxidation with a mild oxidising agent like Br2/H20, the glucose is oxidized to
saccharic acid
glucaric acid
gluconic acid
valeric acid
10
Multiple Choice
Glycosidic linkage is an
amide linkage
ester linkage
ether linkage
acetyl linkage
11
Multiple Choice
The letter ‘D’ in carbohydrates signifies
dextrorotatory
configuration
diamagnetic nature
mode of synthesis
12
Multiple Choice
Maltose is made up of
two α-D-glucose
normal β-D-glucose
α- and β-D-glucose
fructose
13
Multiple Choice
Which of the following treatment will convert starch directly into glucose?
Heating with dilute H2SO4
Fermentation by diastase
Fermentation by zymase
Heating with dilute NaOH
14
Proteins
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Acidic amino acids
Basic amino acids
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20
Multiple Choice
If a methyl group (-CH3), which does not like water, were at the 'R', the amino acid would likely be:
Hydrophobic
Hydrophilic
Ionic
Acidic
21
Multiple Choice
22
Multiple Choice
23
Multiple Choice
24
Multiple Select
All hydrophobic aminoacids (valine, leucine, isoleucine etc) share which of the following properties?
polar uncharged R-groups
non-polar uncharged R-groups
25
Multiple Choice
When R is H, then amino acid is....................
Serine
Glycine
Alanine
Lysine
26
Multiple Choice
Which of the following amino acids is essential amino acid
Asparagine
Threonine
Serine
Cysteine
27
Multiple Choice
The amino acids, which can be synthesised in the body, are known as ................
essential amino acids
non- essential amino acids
28
Multiple Choice
Except glycine, all other naturally occurring α-amino acids are optically ..............., since the α-carbon atom is ...........................
active, symmetric
inactive, symmetric
active, asymmetric
inactive, asymmetric
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34
Multiple Choice
Amino acids are usually ..........................solids.
crystalline
amorphous
35
Multiple Choice
Amino acids are ................
water soluble
water insoluble
sparingly soluble in water
36
Multiple Choice
In zwitter ionic form, amino acids show ..............................behaviour
acidic
basic
amphoteric
37
Multiple Choice
proteins are the polymers of α-amino acids and they are connected to each other by ........................
glycosidic bond
covalent bond
dative bond
peptide bond
38
Multiple Choice
Chemically, peptide linkage is an ........................formed between –COOH group and –NH2 group
amine
ether
amide
ester
39
Multiple Choice
If a third amino acid combines to a ..........................., the product is called a .....................
dipeptide, tripeptide
dipeptide, dipeptide
tripeptide, tripeptide
tripeptide, dipeptide
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46
Multiple Choice
47
Multiple Choice
48
Multiple Choice
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Multiple Choice
50
Multiple Choice
Are these statements about amino acids true or false?
Peptide links can undergo hydrolysis by reflux with hydrochloric acid
true
false
51
Multiple Choice
Why are many enzymes soluble in water?
They contain large numbers of hydrogen bonds
They contain many amino acids with hydrophilic side chains
they contain an active site
52
Multiple Choice
Which one is an acidic amino acid?
53
Multiple Choice
54
Multiple Choice
Why is folding so important in proteins?
It gives them a unique, 3-D functional shape
It makes them look tidier
It makes every protein molecule different from the next even if they are the same type
The folding is random so is not that important at all
55
Multiple Choice
The main bonding in the secondary structure of a protein is due to.....
covalent bonding
ionic bonding
hydrogen bonding
polar bonding
56
Multiple Choice
Shape is essential for a protein to be functional?
57
Multiple Select
Which of the following give a protein its unique 3-D shape? (3)
the unique sequence of amino acids in the primary structure
hydrogen bonding to form alpha-helixes and beta-pleated sheets in the secondary structure.
unique interactions between the 'R' groups in the tertiary structure
random folding due to temperature and extreme pH throughout the folding process
unique sequence of monosaccharides in the quaternary structure
Biomolecules
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