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The gramicidin A channel
Author(s) -
Etchebest Catherine,
Pullman Alberte
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80824-9
Subject(s) - gramicidin , ethanolamine , chemistry , channel (broadcasting) , ion channel , ion , crystallography , stereochemistry , biophysics , biochemistry , biology , membrane , telecommunications , organic chemistry , receptor , computer science
The effect of the conformational freedom of the ethanolamine tail of gramicidin A on the energy profile for the transfer of Na + , computed in the presence of water, shows an appreciable lowering of the minimum at 10.5 Å, and a splitting of the entrance barrier. The deep energy region at the channel mouth remains, however, the deepest one and contains a site of strong interaction of the ion with the Trp 11 carbonyl, at about 12 Å from the center.