PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein wza from escherichia coli.

Gregor Hagelueken; W. John Ingledew; Hexian Huang; Biljana Petrovic-Stojanovska; Chris Whitfield; Hassane ElMkami; Olav Schiemann; James H. Naismith

doi:10.1002/anie.200805758

PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein wza from escherichia coli.

Gregor Hagelueken
, W. John Ingledew
, Hexian Huang
, Biljana Petrovic-Stojanovska
, Chris Whitfield
, Hassane ElMkami
, Olav Schiemann
, James H. Naismith

Research output: Contribution to journal › Article › peer-review

62 Scopus citations

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.

Original language	English
Pages (from-to)	2904-2906
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	16
DOIs	https://doi.org/10.1002/anie.200805758
State	Published - 6 Apr 2009
Externally published	Yes

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10.1002/anie.200805758

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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.",

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AU - Hagelueken, Gregor

AU - Ingledew, W. John

AU - Huang, Hexian

AU - Petrovic-Stojanovska, Biljana

AU - Whitfield, Chris

AU - ElMkami, Hassane

AU - Schiemann, Olav

AU - Naismith, James H.

PY - 2009/4/6

Y1 - 2009/4/6

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AB - 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.

UR - https://www.scopus.com/pages/publications/70349777756

U2 - 10.1002/anie.200805758

DO - 10.1002/anie.200805758

M3 - Article

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AN - SCOPUS:70349777756

SN - 1433-7851

VL - 48

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 16

ER -

PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein wza from escherichia coli.

Abstract

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