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On the Function and Structure of Synthetically Modified Porins
Author(s) -
Reitz Simon,
Cebi Menekse,
Reiß Philipp,
Studnik Gregor,
Linne Uwe,
Koert Ulrich,
Essen LarsOliver
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200900457
Subject(s) - trimer , porin , biophysics , chemistry , ion channel , crystallography , nanotechnology , stereochemistry , materials science , biology , biochemistry , receptor , bacterial outer membrane , dimer , organic chemistry , escherichia coli , gene
The attachment of modulators to a trimeric porin ion channel was investigated (see picture of the trimer with a crown ether modulator (orange)). The interplay of modulator and protein is essential for the conformational heterogeneity of the hybrid channel. Single‐site attachment in large pores is not sufficient to change the electrophysiological characteristics of the pores—such change requires additional noncovalent interactions or second‐site attachments.