Worksheets1.4 Proteins
Total questions: 15
Worksheet time: 20mins
if four amino acids condensed together, how many peptide bonds are formed?
4
3
5
2
Which type of bond stabilize the α-helix and β-pleated sheet structures of proteins?
peptide bonds
disulfide bridge
hydrogen bonds
ionic bonds
An α-helix is which level of protein structure
primary
secondary
tertiary
quaternary
Polymers of polysaccharides, proteins and nucleic acid are all synthesised from monomers by
hydration.
condensation.
carboxylation.
hydrolysis
The unique characteristic of each amino acid is determined by
the type of peptide bond.
its position on the polypeptide chain.
its amino group.
its R group
Amino acids can be classified into different groups. Which is NOT one of the groups?
Non-polar
Acidic
Amphoteric
Basic
At which levels of protein structure do hydrophobic interactions occur?
Quaternary only
Tertiary and quaternary.
Primary, secondary and tertiary
Primary, secondary, tertiary and quaternary.
Amino acid is an amphoteric molecule because
it consist of both positive and negative charges
it consist of both acidic and basic groups
it consist of both nitrogen and carbon group
it consist of hydrophobic and hydrophilic region
A peptide bond is formed between
an aldehyde group and an amino group
an aldehyde group and carboxyl group
a carboxyl group and an amino group
a carboxyl group and ester group
Myoglobin is an example of protein with _____________________
primary structure
secondary structure
tertiary structure
quaternary structure
Which of the following bonds is NOT affected when a protein denatures?
van der Waals interaction
hydrogen bond
peptide bond
ionic bond
Which of the following are the effects of extreme pH exposure on protein structure?
(the correct answer can be more than one)
Hydrogen bond is disrupted in secondary structure
Will causes breakage of hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interaction and van der Waals interactions
3D structure of protein is unstable due to breakage of the ionic bonds
Denatured protein will lose its biological activities and becomes nonfunctioning
