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Structural investigations of pneumolysin/lipid complexes.

Abstract:

Pneumolysin, a virulence factor from the human pathogen Streptococcus pneumoniae, is a water-soluble protein which forms ring-shaped oligomeric structures upon binding to cholesterol-containing lipid membranes. It induces vesicle aggregation, membrane pore formation and withdrawal of lipid material into non-bilayer proteolipid complexes. Solid-state magic angle spinning and wideline static NMR, together with freeze-fracture electron microscopy, are used to characterize the phase changes in fu...

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Publication status:
Published

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Publisher copy:
10.1080/09687680010018394

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Molecular membrane biology
Volume:
17
Issue:
4
Pages:
229-235
Publication date:
2000-01-01
DOI:
EISSN:
1464-5203
ISSN:
0968-7688
URN:
uuid:a1603fd1-e82b-46d8-88a4-cc6b75779c00
Source identifiers:
100235
Local pid:
pubs:100235

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