Article
The effect of point mutations on energy profiles in a model of the nicotinic acetylcholine receptor (AChR) channel.
Biophysical chemistry - 1 Feb 1991
Furois-Corbin S, Pullman A
Abstract excerpt
Energy profiles are calculated, using energy optimization computations, for a sodium cation in the AChR channel and four of its mutants, alpha E241D, beta E247Q, delta E255Q and alpha E241Q, using the model developed previously. The relative energy location of the calculated profiles confirms and specifies the role of each of the Glu residues found in the anionic ring at the bottom of the MII helices. The...
Topics
- Amino Acid Sequence
- Animals
- Chemical Phenomena
- Chemistry, Physical
- Models, Chemical
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Receptors, Nicotinic
- Sodium
- Thermodynamics
