## Abstract We examined CH/π hydrogen bonds in protein/ligand complexes involving at least one proline residue using the __ab initio__ fragment molecular orbital (FMO) method and the program CHPI. FMO calculations were carried out at the Hartree–Fock (HF)/6‐31G\*, HF/6‐31G\*\*, second‐order Møller–
CH/π hydrogen bonds as evidenced in the substrate specificity of acetylcholine esterase
✍ Scribed by Yoji Umezawa; Motohiro Nishio
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2005
- Tongue
- English
- Weight
- 362 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The crystal structure of acetylcholine esterase (AchE) in complex with various inhibitors, investigated as drugs for improvement of the cognitive ability of early stage Alzheimer's disease, has been analyzed with the use of our program CHPI. A number of CH/π hydrogen bonds have been disclosed in the binding of the inhibitors with Torpedo californica AchE. It has been demonstrated that, in order to be effective in the binding with AchE, C—H bonds in the inhibitor need not be polarized. © 2005 Wiley Periodicals, Inc. Biopolymers 79: 248–258, 2005
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
📜 SIMILAR VOLUMES
## Abstract A systematic study was carried out to understand the principle underlying the process of enantiomeric resolution by the use of the Cambridge Structural Database. The crystal structures of fourteen pairs of diastereomeric salts, containing the mandelate anion, or its analogues, as the ch