0000000000742968

AUTHOR

Zoé Joly-lopez

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Refolding of the integral membrane protein light-harvesting complex II monitored by pulse EPR

2009

The major light-harvesting chlorophyll a / b complex (LHCII) of the photosynthetic apparatus in plants self-organizes in vitro. The recombinant apoprotein, denatured in dodecyl sulfate, spontaneously folds when it is mixed with its pigments, chlorophylls, and carotenoids in detergent solution, and assembles into structurally authentic LHCII in the course of several minutes. Pulse EPR techniques, specifically double-electron-electron resonance (DEER), have been used to analyze protein folding during this process. Pairs of nitroxide labels were introduced site-specifically into recombinant LHCII and shown not to affect the stability and function of the pigment-protein complex. Interspin dist…

Protein DenaturationProtein FoldingTime FactorsMultidisciplinaryPulsed EPRSuperhelixChemistryElectron Spin Resonance SpectroscopyLight-Harvesting Protein ComplexesPeasMembrane ProteinsElectronsBiological SciencesModels BiologicalProtein Structure SecondaryTransmembrane domainB vitaminsCrystallographyProtein structureMutationHelixSpin LabelsProtein foldingApoproteinsIntegral membrane proteinProceedings of the National Academy of Sciences
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