Publication Date:
1996-01-12
Description:
Cations bind to the pi face of an aromatic structure through a surprisingly strong, non-covalent force termed the cation-pi interaction. The magnitude and generality of the effect have been established by gas-phase measurements and by studies of model receptors in aqueous media. To first order, the interaction can be considered an electrostatic attraction between a positive charge and the quadrupole moment of the aromatic. A great deal of direct and circumstantial evidence indicates that cation-pi interactions are important in a variety of proteins that bind cationic ligands or substrates. In this context, the amino acids phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) can be viewed as polar, yet hydrophobic, residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dougherty, D A -- GM43936/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):163-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539615" target="_blank"〉PubMed〈/a〉
Keywords:
Acetylcholine/metabolism
;
Benzene/chemistry/*metabolism
;
Binding Sites
;
Cations/chemistry/*metabolism
;
Chemistry, Physical
;
Ion Channels/metabolism
;
Phenylalanine/chemistry/*metabolism
;
Physicochemical Phenomena
;
Proteins/*metabolism
;
Receptors, Cholinergic/metabolism
;
Steroids/biosynthesis
;
Tryptophan/chemistry/*metabolism
;
Tyrosine/chemistry/*metabolism
;
Water/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
