Premium
Thermal stability of outer membrane protein porin from Paracoccus denitrificans : FT‐IR as a spectroscopic tool to study lipid–protein interaction
Author(s) -
Sukumaran Suja,
Hauser Karin,
Rauscher Annette,
Mäntele Werner
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.059
Subject(s) - porin , paracoccus denitrificans , bacterial outer membrane , lipid bilayer , chemistry , bilayer , biophysics , membrane protein , membrane , thermal stability , biochemistry , biology , organic chemistry , escherichia coli , gene , enzyme
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.