A mutation of Lys to Phe in a protein causes the protein no longer bind it's substrate. The substrate contains several functional groups important for binding to the protein. The mutation of the protein would likely disrupt the binding to which type of functional group?

Question

Adam Holden

Biology

4 August, 00:06

A mutation of Lys to Phe in a protein causes the protein no longer bind it's substrate. The substrate contains several functional groups important for binding to the protein. The mutation of the protein would likely disrupt the binding to which type of functional group?

+1

Answers (1)

Know the Answer?

Maren Peterson · Answer 1

It would disrupt binding to negatively charged functional groups.

Explanation:

The lysine side chain contains an amino group (-NH3) that is usually protonated under physiolgoical pH (-NH4+), making it positively charged and basic. This enables it to interact with negatively charged functional groups (e. g. deprotonated acids, - COO-). Phenylalanine contains an aromatic ring but no charged functional groups in its side chain. Therefore, a mutation from Lys to Phe would prevent interaction with negatively charged functional groups.