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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Detergents / pharmacology
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Genetic Vectors
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Lipid Bilayers / chemistry
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Lipid Bilayers / metabolism
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Lipid Metabolism*
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Lipoproteins / metabolism
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Liposomes / chemistry
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Membrane Proteins / chemistry*
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Membrane Proteins / drug effects
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Membrane Proteins / genetics
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Micelles
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Models, Molecular
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Paracoccus denitrificans / genetics
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Paracoccus denitrificans / metabolism*
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Phosphatidylcholines / chemistry
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Phosphatidylcholines / metabolism
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Porins / chemistry
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Porins / genetics
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Porins / isolation & purification
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Porins / metabolism*
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Protein Structure, Secondary
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Proteins / metabolism*
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Spectroscopy, Fourier Transform Infrared*
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Temperature
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Tyrosine / chemistry
Substances
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Detergents
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Lipid Bilayers
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Lipoproteins
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Liposomes
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Membrane Proteins
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Micelles
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Phosphatidylcholines
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Porins
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Proteins
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Tyrosine