PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli.
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.
Hagelueken
Gregor
G
Centre for Biomolecular Sciences, The University of St. Andrews, Fife KY16 9RH, UK.
Ingledew
W John
WJ
Huang
Hexian
H
Petrovic-Stojanovska
Biljana
B
Whitfield
Chris
C
ElMkami
Hassane
H
Schiemann
Olav
O
Naismith
James H
JH
D019943:Amino Acid Substitution; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D050505:Mutant Proteins / Q000737:chemistry; D019897:Periplasm / Q000378:metabolism; D017434:Protein Structure, Tertiary
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D050505:Mutant Proteins; C404158:Wza protein, E coli