title: Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel.
abstract: Lipid-protein interactions, critical for the folding, stability and function of membrane proteins, can be both of mechanical and chemical nature. Mechanical properties of lipid systems can be suitably influenced by physical factors so as to facilitate membrane protein folding. We demonstrate here that by modulating lipid dynamics transiently using heat, rapid folding of two 8-stranded transmembrane β-barrel proteins OmpX and OmpA(1-171), in micelles and vesicles, can be achieved within seconds. Folding kinetics using this 'heat shock' method shows a dramatic ten to several hundred folds increase in refolding rate along with ~100% folding efficiency. We establish that OmpX thus folded is highly thermostable even in detergent micelles, and retains structural characteristics comparable to the protein in bilayers.
authors.affiliation: Department of Biological Sciences, Indian Institute of Science Education and Research, Govindpura, Bhopal, India.
authors.forename: Svetlana Rajkumar
authors.initials: SR
authors.lastname: Maurya
authors.forename: Deepti
authors.initials: D
authors.lastname: Chaturvedi
authors.forename: Radhakrishnan
authors.initials: R
authors.lastname: Mahalakshmi
mesh_terms: D002942:Circular Dichroism; D007700:Kinetics; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D008563:Membrane Lipids