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Expanding the Scope of Protein Trans ‐Splicing to Fragment Ligation of an Integral Membrane Protein: Towards Modulation of Porin‐Based Ion Channels by Chemical Modification
Author(s) -
Brenzel Steffen,
Cebi Menekse,
Reiß Philipp,
Koert Ulrich,
Mootz Henning D.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900039
Subject(s) - porin , chemistry , ligation , integral membrane protein , ion channel , biophysics , rna splicing , membrane protein , membrane , biochemistry , biology , bacterial outer membrane , gene , microbiology and biotechnology , receptor , rna , escherichia coli
It's raining, it's porin : Fragment ligation of OmpF ion channels was achieved by using the split Psp ‐GBD Pol intein; this allowed reconstitution of active trimeric porin. In combination with cysteine modification at an internal position, the porin's conductance properties were altered.