Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Bacterial Outer Membrane Proteins / chemistry*
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Computer Simulation
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Crystallography, X-Ray
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Electron Spin Resonance Spectroscopy
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Escherichia coli / chemistry*
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Escherichia coli Proteins / chemistry*
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Mutant Proteins / chemistry
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Periplasm / metabolism
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Protein Structure, Tertiary
Substances
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Bacterial Outer Membrane Proteins
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Escherichia coli Proteins
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Mutant Proteins
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Wza protein, E coli