Answered: 1 0.8 0.6 Mutant y 0.4 Wild-Type 0.2 40…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Question

You are working with a protein that is known to form an functioning complex of three identical polypeptide subunits, each with a binding site for a ligand of interest. You are studying an inherited mutation in the protein that changes one Asp residue to a Leu residue in each subunit. A comparison of the binding curves for the normal (wild-type) and mutant versions of the complex are shown below. Suggest a mechanism for the effect that this mutation has on the structure of the complex.

1
0.8
0.6
Mutant
y
0.4
Wild-Type
0.2
20
40
60
80
[ligand]

Expert Solution

Step 1

According to the given information, the wild type protein structure has aspartate in its primary structure. This aspartate is changed to leucine inthe mutant form of protein.

These wild type and mutant proteins differ in their binding affinities with ligand which is shown in binding curves of wild type and mutant proteins.