0000000000164980

AUTHOR

Steven J. Roeters

0000-0003-3238-2181

showing 3 related works from this author

IM30 triggers membrane fusion in cyanobacteria and chloroplasts

2015

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg2+, membr…

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein BindingNature Communications
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Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy

2021

High-resolution structural information on membrane proteins is essential for understanding cell biology and for the structure-based design of new medical drugs and drug delivery strategies. X-ray diffraction (XRD) can provide angstrom-level information about the structure of membrane proteins, yet for XRD experiments, proteins are removed from their native membrane environment, chemically stabilized, and crystallized, all of which can compromise the conformation. Here, we describe how a combination of surface-sensitive vibrational spectroscopy and molecular dynamics simulations can account for the native membrane environment. We observe the structure of a glycerol facilitator channel (GlpF)…

GlycerolInfrared spectroscopyAquaporinPROTEINAquaporinsVIBRATIONAL SPECTROSCOPYMolecular dynamicsCHANNELElectrochemistryGeneral Materials SciencePEPTIDESpectroscopyCRYSTALChemistryEscherichia coli ProteinsSpectrum AnalysisMembrane structureWaterSurfaces and InterfacesCondensed Matter PhysicsBILAYERGLYCEROLINTERFACEMembraneMembrane proteinMOLECULAR-DYNAMICSBiophysicsMembrane channelORIENTATIONSum frequency generation spectroscopy
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Peptide-Controlled Assembly of Macroscopic Calcium Oxalate Nanosheets

2019

The fabrication of two-dimensional (2D) biomineral nanosheets is of high interest owing to their promise for applications in electronics, filtration, catalysis, and chemical sensing. Using a facile approach inspired by biomineralization in nature, we fabricate laterally macroscopic calcium oxalate nanosheets using β-folded peptides. The template peptides are composed of repetitive glutamic acid and leucine amino acids, self-organized at the air-water interface. Surface-specific sum frequency generation spectroscopy and molecular dynamics simulations reveal that the formation of oxalate nanosheets relies on the peptide-Ca 2+ ion interaction at the interface, which not only restructures the …

chemistry.chemical_classificationLetterMaterials scienceFabricationHigh interestCalcium oxalatePeptideCatalysislaw.inventionchemistry.chemical_compoundchemistryChemical engineeringlawGeneral Materials SciencePhysical and Theoretical ChemistryFiltrationThe Journal of Physical Chemistry Letters
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