Malleability of the Folding Mechanism of the Outer Membrane Protein PagP: Parallel Pathways and the Effect of Membrane Elasticity
作者： Gerard H.M. Huysmans , Sheena E. Radford , Stephen A. Baldwin , David J. Brockwell
DOI: 10.1016/J.JMB.2011.12.039
关键词: Bacterial outer membrane 、 Biochemistry 、 Cell membrane 、 Membrane 、 Membrane protein 、 Lipid bilayer 、 Liposome 、 Biophysics 、 Protein structure 、 Chemistry 、 Protein folding 、 Molecular biology
摘要: Understanding the interactions between membrane proteins and lipid bilayer is key to increasing our ability predict tailor folding mechanism, structure stability of proteins. Here, we have investigated effects changing composition relative concentrations protein on mechanism bacterial outer PagP. The pathway, monitored by tryptophan fluorescence, was found be characterized a burst phase, representing PagP adsorption liposome surface, followed time course that reflects insertion into membrane. In 1,2-dilauroyl-sn-glycero-3-phosphocholine (diC12:0PC) liposomes, post-adsorption fits well single exponential at high lipid-to-protein ratios (LPRs), but low LPRs, second phase with slower rate constant observed. Interrupted refolding assays demonstrated two phases reflect presence parallel pathways. Partitioning these pathways modulated elastic properties Folding mixed 1,2-dilauroyl-sn-glycero-3-phosphoethanolamine:diC12:0PC liposomes resulted in decrease switch pathway. By contrast, inclusion 1,2-dilauroyl-sn-glycero-3-phosphoserine diC12:0PC fast results highlight effect tailoring protein, revealing access multiple, competing routes unique native structure.
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