Physical organic chemistry in the brain
- Creators
-
Dougherty, Dennis A.
Abstract
A new tool for precise structural modification of ion channel proteins - the in vivo nonsense suppression technique for incorporating unnatural amino acids - has been developed. This new tool allows the kind of systematic structure-function correlation studies that are commonly employed in physical organic chemistry to be applied to the important proteins of molecular neurobiology. In particular, the method has been applied to the nicotinic acetylcholine receptor, The differing roles of the numerous aromatic amino acids present at the agonist binding site can be distinguished. In addition, high precision studies of the ion channel region have produced new insights into the channel gating mechanism.
Additional Information
© 1997 IUPAC. I thank my colleague and collaborator Henry Lester for invaluable contributions to this work. I also thank the many outstanding graduate students and postdocs who have been part of the "unnatural group". Our work in this area has been supported by the National Institutes of Health (NS34407).Attached Files
Published - _Pure_and_Applied_Chemistry__Physical_organic_chemistry_in_the_brain.pdf
Files
| Name | Size | Download all |
|---|---|---|
|
md5:8c6f320ed08c3590f51b3c37306ceb86
|
663.1 kB | Preview Download |
Additional details
- Eprint ID
- 88718
- Resolver ID
- CaltechAUTHORS:20180809-152106261
- NIH
- NS34407
- Created
-
2018-08-09Created from EPrint's datestamp field
- Updated
-
2021-11-16Created from EPrint's last_modified field