Kernen P Gruszecki WI Matuta M Wagner P Ziegler U Krupa Z 1998 Monomolecular layers at the air-water interface were formed directly with isolated largest light-harvesting pigment-protein complex of Photosystem II (LHC II) or out of egg yolk lecithin (EYL) liposomes containing incorporated LHC II. Pure protein monolayers showed a mean area of 1400 A2 per molecule at the air-water interface. Monolayers were deposited onto glass slides by means of Langmuir-Blodgett (LB) technique. Chlorophyll fluorescence of LHC II-LB and EYL-LHC II-LB films proved energetic coupling of chlorophyll a and b, thus indicating native conformation of LHC II within the monolayers. Scanning force microscopy (SFM) revealed ring-like structures formed in monocomponent protein layers as well as in mixed protein-lipid films. These results suggest that a structural arrangement of LHC II is favoured in a lipid environment but that the protein has itself a strong tendency for structural complex rearrangement in our system. https://sonar.ch/global/documents/61451 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/s0005-2736(98)00109-6 info:eu-repo/semantics/altIdentifier/pmid/9733986 Biochimica et biophysica acta. - 1998 Chlorophyll Light-Harvesting Protein Complexes Lipid Metabolism Liposomes Membrane Proteins Microscopy, Atomic Force Phosphatidylcholines Photosynthetic Reaction Center Complex Proteins Photosystem II Protein Complex Plant Leaves Plant Proteins Pressure Protein Conformation Secale Spectrometry, Fluorescence Spectrophotometry Surface Properties Light-harvesting complex II in monocomponent and mixed lipid-protein monolayers. http://purl.org/coar/resource_type/c_6501