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PELDOR Spectroscopy Distance Fingerprinting of the Octameric Outer‐Membrane Protein Wza from Escherichia coli .
Author(s) -
Hagelueken Gregor,
Ingledew W. John,
Huang Hexian,
PetrovicStojanovska Biljana,
Whitfield Chris,
ElMkami Hassane,
Schiemann Olav,
Naismith James H.
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.200805758
Subject(s) - periplasmic space , chemistry , spectroscopy , bacterial outer membrane , crystallography , escherichia coli , membrane , biophysics , biochemistry , biology , physics , quantum mechanics , gene
Distance fingerprinting : Pulsed electron–electron double resonance spectroscopy (PELDOR) is applied to the octameric membrane protein complex Wza of E. coli. The data yielded a detailed distance fingerprint of its periplasmic region that compares favorably to the crystal structure. These results provide the foundation to study conformation changes from interaction with partner proteins.