Publikation: Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction
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2005
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FEBS Letters. 2005, 579(12), pp. 2546-2550. ISSN 0014-5793. Available under: doi: 10.1016/j.febslet.2005.03.059
Zusammenfassung
Abstract Lipid protein interactions play a key role in the stability and function of various membrane proteins. Earlier we have reported the extreme thermal stability of porin from Paracoccus denitrificans reconstituted into liposomes. Here, we used Fourier transform infrared spectroscopy for a label free analysis of the global secondary structural changes and local changes in the tyrosine microenvironment. Our results show that a mixed lipid system (non-uniform bilayer) optimizes the thermal stability of porin as compared to the porin in pure lipids (uniform bilayer) or detergent micelles. This is in line with the fact that the bacterial outer membrane is a dynamic system made up of lipids of varying chain lengths, head groups and the barrel wall height contacting the membrane is uneven.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
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Porin, Membrane protein stability, Lipid-protein interaction, Fourier transform infrared spectroscopy
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SUKUMARAN, Suja, Karin HAUSER, Annette RAUSCHER, Werner MÄNTELE, 2005. Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction. In: FEBS Letters. 2005, 579(12), pp. 2546-2550. ISSN 0014-5793. Available under: doi: 10.1016/j.febslet.2005.03.059BibTex
@article{Sukumaran2005-05-09Therm-17552,
year={2005},
doi={10.1016/j.febslet.2005.03.059},
title={Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT-IR as a spectroscopic tool to study lipid-protein interaction},
number={12},
volume={579},
issn={0014-5793},
journal={FEBS Letters},
pages={2546--2550},
author={Sukumaran, Suja and Hauser, Karin and Rauscher, Annette and Mäntele, Werner}
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