Publikation: Structure–function correlation of outer membrane protein porin from paracoccus denitrificans
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2006
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Biopolymers. 2006, 82(4), pp. 344-348. ISSN 0006-3525. Available under: doi: 10.1002/bip.20422
Zusammenfassung
Porins from outer membrane of Gram-negative bacteria have a highly stable structure. Our previous studies on porin from Paracoccus denitrificans showed that the outer membrane protein porin is extremely stable toward heat, pH, and chemical denaturants. The major question we have addressed in this paper is whether the high stability of porin is a consequence of the b-barrel structure and whether it is required for its function. To explain this we have analyzed two cases: first, we used porin wild-type and mutants and compared their structure and function; second, we compared the activity of porin preheated to different temperatures. Structural changes were monitored by infrared spectroscopy. We observed that the structural stability of porin is not equivalent to functional activity as minor alteration in the structure can result in drastic differences in the activity of porins.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
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porin, structural stability, functional activity, infrared spectroscopy
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SUKUMARAN, Suja, Karin HAUSER, Elke MAIER, Roland BENZ, Werner MÄNTELE, 2006. Structure–function correlation of outer membrane protein porin from paracoccus denitrificans. In: Biopolymers. 2006, 82(4), pp. 344-348. ISSN 0006-3525. Available under: doi: 10.1002/bip.20422BibTex
@article{Sukumaran2006-07Struc-17551,
year={2006},
doi={10.1002/bip.20422},
title={Structure–function correlation of outer membrane protein porin from paracoccus denitrificans},
number={4},
volume={82},
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journal={Biopolymers},
pages={344--348},
author={Sukumaran, Suja and Hauser, Karin and Maier, Elke and Benz, Roland and Mäntele, Werner}
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<dcterms:abstract xml:lang="eng">Porins from outer membrane of Gram-negative bacteria have a highly stable structure. Our previous studies on porin from Paracoccus denitrificans showed that the outer membrane protein porin is extremely stable toward heat, pH, and chemical denaturants. The major question we have addressed in this paper is whether the high stability of porin is a consequence of the b-barrel structure and whether it is required for its function. To explain this we have analyzed two cases: first, we used porin wild-type and mutants and compared their structure and function; second, we compared the activity of porin preheated to different temperatures. Structural changes were monitored by infrared spectroscopy. We observed that the structural stability of porin is not equivalent to functional activity as minor alteration in the structure can result in drastic differences in the activity of porins.</dcterms:abstract>
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