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15 questions
Which of the following describes the secondary structure of proteins?
The sequence of amino acids
The α-helix and β-pleated sheet folding
The folding of the polypeptide chain due to the 'R' groups
The joining of different protein molecules to make one big molecule
Why is folding so important in proteins?
It gives them a unique, 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
The tertiary structure folding in proteins is primary due to the interactions of....
the 'R' groups
the 'P' groups
the 'A' groups
the 'S'
The main bonding in the secondary structure of a protein is due to.....
covalent bonding
ionic bonding
hydrogen bonding
polar bonding
The entire protein forms a three-dimensional structure
primary
secondary
tertiary
quaternary
Tertiary protein structures are mainly maintained by
hydrogen bond
disulfide bridges
covalent bonds
all of the above
Two or more polypeptides attached together and work as one unit
primary structure
secondary structure
quaternary structure
tertiary structure
The primary structure of a protein is a ____ linked together by ____ bonds.
Polypeptide, Peptide
Dipeptide, Hydrogen
Polygon, Covalent
Peptidoglycan, Ionic
There are a total of
12 Amino Acids
64 Amino Acids
24 Amino Acids
20 Amino Acids
The bonding of two amino acid molecules to form a larger molecule requires which of the following?
Addition of a water molecule
Removal of a water molecule
Addition of a glycosidic bond
Formation of a hydrogen bond
Haemoglobin is a quartenary protein because;
It has more than one peptide bonds
Its shape is globular
It consists of more than one polypeptide chains
It has iron in each heme group
The diagram shows a bond forming between two amino acids. What is the name of this reaction?
Condensation
Hydrolysis
Pepysis
Oxidation
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