Article
Conservative and nonconservative mutations in proteins: anomalous mutations in a transport receptor analyzed by free energy and quantum chemical calculations.
Protein science : a publication of the Protein Society - 1 Mar 1995
Cannon W R, Briggs J M, Shen J, McCammon J A, Quiocho F A
Abstract excerpt
Experimental studies on a bacterial sulfate receptor have indicated anomalous relative binding affinities for the mutations Ser130-->Cys,Ser130-->Gly, and Ser130-->Ala. The loss of affinity for sulfate in the former mutation was previously attributed to a greater steric effect on the part of the Cys side chain relative to the Ser side chain, whereas the relatively small loss of binding affinity for the latter two...
Topics
- Bacterial Proteins
- Biological Transport
- Carrier Proteins
- Computer Simulation
- Conserved Sequence
- Models, Chemical
- Models, Molecular
- Mutation
- Periplasmic Binding Proteins
- Sulfates