Search results for "Cell Biophysics"

showing 3 items of 3 documents

Functional rearrangement of the light-harvesting antenna upon state transitions in a green alga

2014

AbstractState transitions in the green alga Chlamydomonas reinhardtii serve to balance excitation energy transfer to photosystem I (PSI) and to photosystem II (PSII) and possibly play a role as a photoprotective mechanism. Thus, light-harvesting complex II (LHCII) can switch between the photosystems consequently transferring more excitation energy to PSII (state 1) or to PSI (state 2) or can end up in LHCII-only domains. In this study, low-temperature (77 K) steady-state and time-resolved fluorescence measured on intact cells of Chlamydomonas reinhardtii shows that independently of the state excitation energy transfer from LHCII to PSI or to PSII occurs on two main timescales of <15 ps and …

0106 biological sciencesPhotosystem IIEnergy transferBiophysicsLight-Harvesting Protein ComplexesphotosystemChlamydomonas reinhardtiiPhotosystem IPhotochemistry01 natural sciences03 medical and health sciencesstate transitionsgreen algaSDG 7 - Affordable and Clean Energy030304 developmental biologyPhotosystem0303 health sciencesenergy transfer/dk/atira/pure/sustainabledevelopmentgoals/affordable_and_clean_energybiologyPhotosystem I Protein ComplexChemistryta1182Photosystem II Protein ComplexState (functional analysis)biology.organism_classificationFluorescenceCell BiophysicsAtomic physicsExcitationChlamydomonas reinhardtii010606 plant biology & botanyBiophysical journal
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GFP-mut2 Proteins in Trehalose-Water Matrixes: Spatially Heterogeneous Protein-Water-Sugar Structures

2007

We report investigations on the properties of nanoenvironments around single-GFP-mut2 proteins in trehalose-water matrixes. Single-GFPmut2 molecules embedded in thin trehalose-water films were characterized in terms of their fluorescence brightness, bleaching dynamics, excited state lifetime, and fluorescence polarization. For each property, sets of approximately 100-150 single molecules have been investigated as a function of trehalose content and hydration. Three distinct and interconverting families of proteins have been found which differ widely in terms of bleaching dynamics, brightness, and fluorescence polarization, whose relative populations sizably depend on sample hydration. The r…

Green Fluorescent ProteinsBiophysicsAnalytical chemistryCarbohydratesMolecular ConformationPhase TransitionColloidchemistry.chemical_compoundMoleculeColloidsSupercoolingthrealosesingle molecule fluorescenceChemistryTrehaloseWaterSingle-molecule experimentFluorescenceTrehaloseSolutionsModels ChemicalChemical physicsCell BiophysicsGFPmut2Excited statelifetimesFluorescence anisotropy
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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009

The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coinci…

Time FactorsLipid BilayersMolecular Sequence DataBiophysicsPeptideFluorescence Polarization7. Clean energy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseErgosterolFluorescence Resonance Energy TransferAmino Acid SequenceLipid bilayer030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeAmyloid beta-PeptidesChemistryCholesterolSterolPeptide FragmentsCrystallographyFörster resonance energy transferMembraneCholesterolCell BiophysicsTyrosinelipids (amino acids peptides and proteins)030217 neurology & neurosurgeryFluorescence anisotropyProtein BindingBiophysical Journal
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