Question

1) Explain why the molecular structures of some lipids makes them useful as detergents (to clean up hydrophobic particles such as oil).

2) An unfolded protein has an almost infinite number of configurations it could adopt, whereas a correctly folded protein has one. Explain, using the concept of multiplicity, which state (folded vs unfolded) is more likely in the absence of any other forces to stabilise the folded state.

Answer 1

Solution

Q1 answer

Because detergents are amhphipathic that is it has polar and non polar composition.

Due to which polar charged and non polar uncharged functional group will bind to oily particle because.

• Oil are made up of lipids having polar (hydrophilic) head and hydrophobic non polar tails.so detergent can wash out or remove out hydrophobic parts due to detergents nonpolar group.because non polar oils always soluble in non polar part of detergent.

Q 2 answer

• Unfolded proteins are like long primary structure of polypeptide.
• Having free and open various R groups, positivly charged negatively charged hydrophobic polar non polar etc .so protein is unstable.
• So there is chance to fold a protein in to multiple confirmation.
• If protein get foled due to R groups then all R group get enagaged in bonding due to hydrogen bonding elalcyrostatic interaction hydrophobic interaction disulphide briges etc.
• So folded protein present in only one possible conformation.and get stabilized.