Berg_2012_Angew.Chem.Int.Ed.Engl_51_12716

Reference

Title : Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase - Berg_2012_Angew.Chem.Int.Ed.Engl_51_12716
Author(s) : Berg L , Niemiec MS , Qian W , Andersson CD , Wittung-Stafshede P , Ekstrom F , Linusson A
Ref : Angew Chem Int Ed Engl , 51 :12716 , 2012
Abstract :

Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein-ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein.

PubMedSearch : Berg_2012_Angew.Chem.Int.Ed.Engl_51_12716
PubMedID: 23161758
Gene_locus related to this paper: mouse-ACHE

Related information

Inhibitor C5685
Gene_locus C5685    mouse-ACHE
Structure C5685    mouse-ACHE    4ARA    4ARB

Citations formats

Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A (2012)
Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase
Angew Chem Int Ed Engl 51 :12716

Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A (2012)
Angew Chem Int Ed Engl 51 :12716