0000000000027991

AUTHOR

Stefan M. Schiller

showing 4 related works from this author

Automated detection of protein unfolding events in atomic force microscopy force curves

2016

Atomic force microscopy is not only a high-resolution imaging device but also a mechanical machine, which can be used either to indent or stretch (soft) biomaterials. Due to the statistical nature of such materials (i.e., hydrogels or polymers) hundreds of force-distance curves are required to describe their mechanical properties. In this manuscript, we present an automated system for polymer unfolding detection based on continuous wavelet analysis. We have tested the automated program on elastin, which is an important protein that provides elasticity to tissues and organs. Our results show that elastin changes its mechanical behavior in the presence of electrolytes. In particular, we show …

0301 basic medicinechemistry.chemical_classificationHistologyMaterials sciencebiologyAtomic force microscopy0206 medical engineeringNanotechnology02 engineering and technologyPolymerAdhesion020601 biomedical engineeringForce curves03 medical and health sciencesMedical Laboratory Technology030104 developmental biologychemistrySelf-healing hydrogelsbiology.proteinContour lengthAnatomyElasticity (economics)Biological systemInstrumentationElastinMicroscopy Research and Technique
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Archaea-analoge Thiolipide für gestützte Lipiddoppelschichtmembranen auf ultraglatten Goldoberflächen

2003

ChemistryGeneral MedicineAngewandte Chemie
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Archaea Analogue Thiolipids for Tethered Bilayer Lipid Membranes on Ultrasmooth Gold Surfaces

2003

biologySurface PropertiesChemistryLipid BilayersMolecular ConformationNanotechnologyBiological membraneGeneral ChemistryModel lipid bilayerbiology.organism_classificationArchaeaCatalysisMembraneBilayer lipid membranesSpectroscopy Fourier Transform InfraredMonolayerBiophysicsGoldSulfhydryl CompoundsSelf-assemblyLipid bilayerArchaeaAngewandte Chemie International Edition
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Dynamic Structural Changes and Thermodynamics in Phase Separation Processes of an Intrinsically Disordered–Ordered Protein Model

2021

Elastin-like proteins (ELPs) are biologically important proteins and models for intrinsically disordered proteins (IDPs) and dynamic structural transitions associated with coacervates and liquid-liquid phase transitions. However, the conformational status below and above coacervation temperature and its role in the phase separation process is still elusive. Employing matrix least-squares global Boltzmann-fitting of the circular dichroism spectra of the ELPs (VPGVG) 20 , (VPGVG) 40 and (VPGVG) 60 , we found that coacervation occurs sharply when a certain number of repeat units has acquired β-turn conformation (in our sequence setting a threshold of ~20 repeat units). The differential scatter…

Models Molecular540 Chemistry and allied sciencesPhase transitionCircular dichroismCoacervateProtein ConformationChemistryPhase separation processCircular DichroismSequence (biology)General ChemistryIntrinsically disordered proteinsCircular dichroism spectraCatalysisIntrinsically Disordered Proteins540 ChemieBiophysicsProtein modelHumansThermodynamicsPeptidesAngewandte Chemie International Edition
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