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Two‐State Folding of the Outer Membrane Protein X into a Lipid Bilayer Membrane
Author(s) -
Rath Parthasarathi,
Sharpe Timothy,
Kohl Bastian,
Hiller Sebastian
Publication year - 2019
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201812321
Subject(s) - membrane , folding (dsp implementation) , lipid bilayer , chemistry , bilayer , protein folding , kinetics , membrane protein , crystallography , biophysics , biochemistry , biology , physics , electrical engineering , engineering , quantum mechanics
Folding and insertion of β‐barrel membrane proteins into native membranes is efficiently catalyzed by β‐barrel assembly machineries. Understanding this catalysis requires a detailed description of the corresponding uncatalyzed folding mechanisms, which however have so far remained largely unclear. Herein, the folding and membrane insertion of the E. coli outer membrane protein X (OmpX) into 1,2‐didecanoyl‐sn‐glycero‐3‐phosphocholine (PC10:0) membranes is resolved at the atomic level. By combining four different experimental techniques, global folding kinetics were correlated with global and local hydrogen bond‐formation kinetics. Under a well‐defined reaction condition, these processes follow single‐exponential velocity laws, with rate constants identical within experimental error. The data thus establish, at atomic resolution, that OmpX folds and inserts into the lipid bilayer of PC10:0 liposomes by a two‐state mechanism.