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OmpT: molecular dynamics simulations of an outer membrane enzyme.

Abstract:

Five molecular dynamics simulations (total duration >25 ns) have been performed on the Escherichia coli outer membrane protease OmpT embedded in a dimyristoylphosphatidylcholine lipid bilayer. Globally the protein is conformationally stable. Some degree of tilt of the beta-barrel is observed relative to the bilayer plane. The greatest degree of conformational flexibility is seen in the extracellular loops. A complex network of fluctuating H-bonds is formed between the active site residues,...

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Publication status:
Published

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Publisher copy:
10.1529/biophysj.104.046987

Authors


Journal:
Biophysical journal
Volume:
87
Issue:
5
Pages:
2942-2953
Publication date:
2004-11-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:4d254aeb-9bf3-46fd-9b67-0c80df23bedf
Source identifiers:
100684
Local pid:
pubs:100684

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