0000000000300189

AUTHOR

Niklas Fehr

showing 3 related works from this author

Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR

2015

The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII mon…

inorganic chemicalsModels MolecularProtein ConformationProtein domainTrimerContext (language use)complex mixturesBiochemistrylaw.inventionchemistry.chemical_compoundBiopolymersProtein structurelawElectron paramagnetic resonanceMolecular BiologySuperhelixfungiElectron Spin Resonance SpectroscopyPhotosystem II Protein ComplexCell Biologyequipment and suppliesCrystallographyMonomerModels ChemicalchemistryThylakoidProtein Structure and FoldingbacteriaJournal of Biological Chemistry
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Comparison of quantum dot-binding protein tags: Affinity determination by ultracentrifugation and FRET

2013

Abstract Background Hybrid complexes of proteins and colloidal semiconductor nanocrystals (quantum dots, QDs) are of increasing interest in various fields of biochemistry and biomedicine, for instance for biolabeling or drug transport. The usefulness of protein–QD complexes for such applications is dependent on the binding specificity and strength of the components. Often the binding properties of these components are difficult and time consuming to assess. Methods In this work we characterized the interaction between recombinant light harvesting chlorophyll a / b complex (LHCII) and CdTe/CdSe/ZnS QDs by using ultracentrifugation and fluorescence resonance energy transfer (FRET) assay exper…

ChemistryBinding proteinBiophysicsNanoparticleProtein tagBiochemistryCrystallographyB vitaminsFörster resonance energy transferQuantum dotQuantum DotsFluorescence Resonance Energy TransferNanoparticlesUltracentrifugeChlorophyll Binding ProteinsUltracentrifugationMolecular BiologyBinding selectivityProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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