Andreas Stadler

ORCID: 0000-0003-2272-5232
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About
Contact & Profiles
Research Areas
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Hemoglobin structure and function
  • Spectroscopy and Quantum Chemical Studies
  • Chalcogenide Semiconductor Thin Films
  • Thin-Film Transistor Technologies
  • Photoreceptor and optogenetics research
  • Photosynthetic Processes and Mechanisms
  • Semiconductor materials and devices
  • ZnO doping and properties
  • Lipid Membrane Structure and Behavior
  • Erythrocyte Function and Pathophysiology
  • NMR spectroscopy and applications
  • Advanced MRI Techniques and Applications
  • Phase-change materials and chalcogenides
  • Advanced NMR Techniques and Applications
  • Gas Sensing Nanomaterials and Sensors
  • Transition Metal Oxide Nanomaterials
  • Quantum Dots Synthesis And Properties
  • Quantum, superfluid, helium dynamics
  • Electron Spin Resonance Studies
  • Crop Yield and Soil Fertility
  • Optical Network Technologies
  • Receptor Mechanisms and Signaling
  • Civil and Structural Engineering Research

Forschungszentrum Jülich
2015-2024

RWTH Aachen University
2019-2024

Institut Laue-Langevin
2007-2021

Stadtwerke Jülich (Germany)
2016-2019

München Klinik
2015-2018

Institute for Complex Systems
2016-2018

E Ink (South Korea)
2017

Prof. Hess Kinderklinik
2016

Hôpital Nord
2016

PTV Group (Germany)
2015

Transparent conducting oxides (TCOs) are electrical conductive materials with comparably low absorption of electromagnetic waves within the visible region spectrum. They usually prepared thin film technologies and used in opto-electrical apparatus such as solar cells, displays, interfaces circuitries. Here, based on a modern database-system, aspects up-to-date material selections applications for transparent sketched, references detailed information given. As n-type TCOs special importance...

10.3390/ma5040661 article EN Materials 2012-04-19

Intrinsically disordered proteins lack a well-defined folded structure and contain high degree of structural freedom conformational flexibility, which is expected to enhance binding their physiological targets. In solution in the lipid-free state, myelin basic protein belongs that class proteins. Using small-angle scattering, was found be structurally similar Gaussian chains. The combination hydrodynamic information revealed an intermediary compactness between globular random coil polymers....

10.1021/ja502343b article EN Journal of the American Chemical Society 2014-04-23

An integrated picture of hydration shell dynamics and its coupling to functional macromolecular motions is proposed from studies on a soluble protein, membrane protein in natural lipid environment, the intracellular environment bacteria red blood cells. Water multimolar salt solutions was also examined, context very slow water component previously discovered cytoplasm extreme halophilic archaea. The data were obtained neutron scattering by using deuterium labelling focus different parts...

10.1039/b805506h article EN Faraday Discussions 2008-11-03

Abstract An overview over the progress in sulfosalts research is given, including basic and application oriented work. The ternary multinary compound semiconductor family defined. chemical composition possibilities are given as well an introduction to structural systematics. peculiarities of complex crystal structures outlined. main characteristics thermodynamic properties exemplarily by SnS–Sb 2 S 3 pseudo‐binary phase diagram. A new Sn–Sb–S system, SnSb 4 7 , reported structure shown....

10.1002/pssa.200881242 article EN physica status solidi (a) 2009-03-12

Guanylate binding proteins (GBPs) are soluble dynamin-like that undergo a conformational transition for GTP-controlled oligomerization and disrupt membranes of intracellular parasites to exert their function as part the innate immune system mammalian cells. We apply neutron spin echo, X-ray scattering, fluorescence, EPR spectroscopy techniques integrative dynamic structural biology study basis mechanism transitions in human GBP1 (hGBP1). mapped hGBP1's essential dynamics from nanoseconds...

10.7554/elife.79565 article EN cc-by eLife 2023-06-14

The dynamics of water in human red blood cells was measured with quasielastic incoherent neutron scattering the temperature range between 290 and 320 K. Neutron spectrometers time resolutions 40, 13, 7 ps were combined to cover scales bulk reduced mobility interfacial motions. A major fraction ∼90% cell is characterized by a translational diffusion coefficient similar water. minor ∼10% cellular exhibits dynamics. This slow attributed dynamically bound on surface hemoglobin which accounts for...

10.1021/ja807691j article EN Journal of the American Chemical Society 2008-11-21

Neutron scattering, by using deuterium labelling, revealed how intracellular water dynamics, measured in vivo E. coli, human red blood cells and the extreme halophile, Haloarcula marismortui, depends on cell type nature of cytoplasm. The method uniquely permits determination motions molecular length (approximately ångstrøm) time (pico- to nanosecond) scales. In bacterial cells, beyond hydration shells cytoplasmic macromolecules membrane faces flows as freely liquid water. It is not "tamed"...

10.1039/c0cp01048k article EN Physical Chemistry Chemical Physics 2010-01-01

Bending and oxygen uptake of a helix copper or gold‐copper alloys, protected at one side by layers silver gold, were measured simultaneously between temperatures 220° 400°C with pressures up to 140 mm Hg. The oxidation mostly showed an induction period then followed logarithmic law. In all cases dilatation the oxide‐covered was first observed, strong contraction. Finally, found again. effects increased if rate lowered, which possible change temperature, pressure, pretreatment metal. stresses...

10.1149/1.2426312 article EN Journal of The Electrochemical Society 1964-01-01

Light, oxygen, voltage (LOV) domains are widely distributed in plants, algae, fungi, bacteria, and represent the photo-responsive of various blue-light photoreceptor proteins. Their photocycle involves triggered adduct formation between C(4a) atom a non-covalently bound flavin chromophore sulfur conserved cysteine LOV sensor domain. proteins show considerable variation structure N- C-terminal elements which flank core domain, as well lifetime state. Here, we report photochemical, structural...

10.1186/s12866-015-0365-0 article EN cc-by BMC Microbiology 2015-02-13

Small-angle X-ray and small-angle neutron scattering (SAXS/SANS) provide unique structural information on biomolecules their complexes in solution. SANS may multiple independent data sets by means of contrast variation experiments, that is, measuring at different D2O concentrations perdeuteration conditions the biomolecular complex. However, even combined from SAXS/SANS is far insufficient to define all degrees freedom a complex, leading significant risk overfitting when refining structures...

10.1021/acs.jctc.9b00292 article EN Journal of Chemical Theory and Computation 2019-06-28

Intrinsically disordered late embryogenesis abundant (LEA) proteins play a central role in the tolerance of plants and other organisms to dehydration brought upon, for example, by freezing temperatures, high salt concentration, drought or desiccation, many LEA have been found stabilize dehydration-sensitive cellular structures. Their conformational ensembles are highly sensitive environment, allowing them undergo changes adopt ordered secondary quaternary structures participate formation...

10.1002/pro.4989 article EN cc-by Protein Science 2024-04-24

This is an immunoradiometric assay of intact human parathyrin, hPTH(1-84). One antibody, directed against the N-terminal part hormone, was produced in goats and conjugated covalently to cellulose particles. hPTH(1-84) fragments were extracted from EDTA-treated plasma by these particles thus concentrated. Another synthetic hPTH(53-84), raised rabbits; this bound C-terminal hormone. The final step labeling second free binding site antibody with 125I-labeled Tyr52-hPTH(53-84) measuring...

10.1093/clinchem/33.8.1376 article EN Clinical Chemistry 1987-08-01

Thermodynamic stability, configurational motions and internal forces of haemoglobin (Hb) three endotherms (platypus, Ornithorhynchus anatinus ; domestic chicken, Gallus gallus domesticus human, Homo sapiens ) an ectotherm (salt water crocodile, Crocodylus porosus were investigated using circular dichroism, incoherent elastic neutron scattering coarse-grained Brownian dynamics simulations. The experimental results from Hb solutions revealed a direct correlation between protein resilience,...

10.1098/rsif.2012.0364 article EN cc-by Journal of The Royal Society Interface 2012-06-13

Binding mechanism of arrestin requires photoactivation and phosphorylation the receptor protein rhodopsin, where bound phosphate groups cause displacement long C-tail 'activating' arrestin. Mutation arginine 175 to glutamic acid (R175E), a central residue in polar core previously predicted as 'phosphosensor' leads pre-active that is able terminate phototransduction by binding non-phosphorylated, light-activated rhodopsin. Here, we report first crystal structure R175E mutant at 2.7 Å...

10.1038/srep15808 article EN cc-by Scientific Reports 2015-10-29

Myoglobin can be trapped in fully folded structures, partially molten globules, and unfolded states under stable equilibrium conditions. Here, we report an experimental study on the conformational dynamics of different apo- holomyoglobin solution. Global protein diffusion internal molecular motions were probed by neutron time-of-flight backscattering spectroscopy picosecond nanosecond time scales. was found to depend α-helical content suggesting that charges macromolecule increase short-time...

10.1039/c6cp04146a article EN cc-by-nc Physical Chemistry Chemical Physics 2016-01-01

A general property of disordered proteins is their structural expansion that results in a high molecular flexibility. The structure and dynamics bovine serum albumin (BSA) denatured by guanidinium hydrochloride (GndCl) were investigated using small-angle neutron scattering (SANS) spin-echo spectroscopy (NSE). SANS experiments demonstrated the relevance intrachain interactions for expansion. Using NSE experiments, we observed internal flexibility BSA addition to center-of-mass diffusion...

10.1021/acs.jpclett.8b00825 article EN The Journal of Physical Chemistry Letters 2018-04-24

Large-scale domain motions in alcohol dehydrogenase (ADH) have been observed previously by neutron spin-echo spectroscopy (NSE). We extended the investigation on dynamics of ADH solution using high-resolution time-of-flight (TOF) and backscattering (BS) incoherent scattering range. The hydrogen were interpreted terms three mobility classes, which allowed a simultaneous description measured TOF BS spectra. In addition to slow global protein diffusion NSE, fast internal process could be...

10.1063/1.4928512 article EN The Journal of Chemical Physics 2015-08-18

Molecular dynamics plays an important role for the biological function of proteins. For protein ligand interactions, changes conformational entropy and hydration layer are relevant binding process. Quasielastic neutron scattering (QENS) was used to investigate differences in ligand-bound ligand-free streptavidin. Protein were probed both on fast picosecond time scale using time-of-flight spectroscopy slower nanosecond high-resolution backscattering spectroscopy. We found internal equilibrium...

10.1021/acs.jpcb.9b08467 article EN The Journal of Physical Chemistry B 2019-11-11

Holo- and apomyoglobin can be stabilized in native folded, partially folded molten globules (MGs) denatured states depending on the solvent composition. Although protein has been studied as a model system field of folding, little is known about internal dynamics different structural conformations picosecond time scale. In comparative experimental study we investigated correlation between folding scale using incoherent quasielastic neutron scattering (QENS). The measured mean square...

10.1021/jp509732q article EN cc-by The Journal of Physical Chemistry B 2014-12-12

We present neutron scattering measurements on the dynamics of haemoglobin (Hb) in human red blood cells (RBCs) vivo . Global and internal Hb were measured ps to ns time Å length scales using quasi-elastic backscattering spectroscopy. observed cross over from global short-time long-time self-diffusion. Both short- diffusion coefficients agree quantitatively with predicted values hydrodynamic theory non-charged hard-sphere suspensions when a bound water fraction around 0.23 gram H 2 O per is...

10.1098/rsif.2010.0306 article EN Journal of The Royal Society Interface 2010-08-25

Abstract Myelin basic protein (MBP) and its interaction with lipids of the myelin sheath plays an important part in pathology multiple sclerosis (MS). Previous studies observed that changes lipid composition lead to instabilities enhanced local curvature MBP-lipid multilayer structures. We investigated molecular origin instability found diseased membrane has a 25% lower bending rigidity, thus destabilizing smooth $$&gt;1\,$$ <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML">...

10.1038/s41598-020-73671-3 article EN cc-by Scientific Reports 2020-10-07

Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the constants. The Soret effect has also been proven be promising tool gain hydration layer, as temperature dependence thermodiffusion is sensitive solute-solvent interactions. In this work, we perform systematic thermophoretic measurements streptavidin (STV) complex STV with biotin (B) using thermal diffusion forced Rayleigh scattering (TDFRS). Our experiments show that sensitivity...

10.3390/polym12020376 article EN Polymers 2020-02-07
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