Practice Questions

TLS Online TPP Program

#Question id: 878

Can a peptide bind more strongly to an unfolded than the same protein in a folded state?

#Unit 1. Structure and Function of Biomolecules

It will depend on the balance of favourable interactions (enthalpy) versus loss in conformational entropy. For the folded protein, the loss in conformational entropy is less upon binding.
If the increased interactions for the unfolded protein can less than compensate the increased loss in conformational entropy then the net Gibbs free energy will be favourable.
The unfolding do not cause the the appearance of hydrophobic sites of the surface of protein, so if the interaction of the peptide with the protein is depending on the hydrophobic site.
If the binding site changed due to unfolding the binding will be stronger.

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TLS Online TPP Program

#Question id: 5754

#Unit 8. Inheritance Biology

A cell is exposed to EMS (a mutagen that causes guanine to mispair with thymine) and allowed to undergo a few rounds of DNA replication. The mutational event caused by this mutagen will be

TLS Online TPP Program

#Question id: 5755

#Unit 8. Inheritance Biology

A researcher studying bacterial toxin predicts that a lysine within the toxin is important for binding it’s target cell. She used site-directed mutagenesis to change a codon for lysine (AAA) to one for asparagine (AAU). However, the mutant toxin still binds to its target cell just as well as the wild-type toxin bound and appears to have no other changes. This type of mutation is probably

TLS Online TPP Program

#Question id: 5756

#Unit 8. Inheritance Biology

Type of mutation caused by an addition or deletion of a base in a polypeptide-encoding part of a gene

TLS Online TPP Program

#Question id: 5757

#Unit 8. Inheritance Biology

A new E. coli mutant was tested for auxotrophy. The mutant grows on:

minimal medium (M) + arginine (A) + proline (P)

M + P + histidine (H)

M + A + H + P

but not on M or on M + A + H. The mutant requires