Stockholm University
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Andreas Barth

Professor in Experimental Molecular Biophysics (Chemical sciences; Physical sciences; Biological sciences)

Stockholm, Sweden

Publications

  • Tracking Ca 2+ ATPase intermediates in real time by x-ray solution scattering
  • Properties of Biomimetic Artificial Spider Silk Fibers Tuned by PostSpin Bath Incubation
  • Quality assessment of recombinant proteins by infrared spectroscopy. Characterisation of a protein aggregation related band of the Ca2+-ATPase
  • Effect of lipid bilayer properties on the photocycle of green proteorhodopsin
  • Microplastic-mediated transport of PCBs? A depuration study with Daphnia magna
  • Inhibition of Protein Synthesis with Highly Soluble Caged Compounds
  • Erratum: Formation of two different types of oligomers in the early phase of pH-induced aggregation of the alzheimer aβ(12-28) peptide (Journal of Physical Chemistry B (2012) 116:41 (12389-12397) DOI: 10.1021/jp305015g)
  • Microplastic Intake, Its Biotic Drivers, and Hydrophobic Organic Contaminant Levels in the Baltic Herring
  • The carbonate/bicarbonate system as a pH indicator for infrared spectroscopy
  • Use of creatine kinase to induce multistep reactions in infrared spectroscopic experiments
  • Rapid Physicochemical Changes in Microplastic Induced by Biofilm Formation
  • Simultaneous fitting of absorption spectra and their second derivatives for an improved analysis of protein infrared spectra
  • Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation
  • Computational de novo design of a self-assembling peptide with predefined structure
  • Capital regulation with heterogeneous banks – Unintended consequences of a too strict leverage ratio
  • Membrane-induced folding of the plant stress dehydrin Lti30
  • Heterologous overexpression of a monotopic glucosyltransferase (MGS) induces fatty acid remodeling in Escherichia coli membranes
  • Probing the activity of a recombinant Zn2+-transporting P-type ATPase
  • Hydrophobic organic contaminants are not linked to microplastic uptake in Baltic Sea herring
  • Risk for the release of an enormous amount of nanoplastics and microplastics from partially biodegradable polymer blends
  • Use of Creatine Kinase to Induce Multi-Step Reactions in Infrared Spectroscopic Experiments.
  • Conformational changes of recombinant Ca2+-ATPase studied by reaction-induced infrared difference spectroscopy.
  • Anionic lipid binding to the foreign protein MGS provides a tight coupling between phospholipid synthesis and protein overexpression in Escherichia coli.
  • Hydrolysis of the E2P phosphoenzyme of the Ca(2+)-ATPase: a theoretical study.
  • Characterization of recombinant antibodies for cancer therapy by infrared spectroscopy.
  • Detection of ligand binding to proteins through observation of hydration water.
  • Formation of two different types of oligomers in the early phase of pH-induced aggregation of the Alzheimer Aβ(12-28) peptide.
  • Coumarin-based octopamine phototriggers and their effects on an insect octopamine receptor.
  • Vibrational coupling between helices influences the amide I infrared absorption of proteins: application to bacteriorhodopsin and rhodopsin.
  • Optimization of Model Parameters for Describing the Amide I Spectrum of a Large Set of Proteins.
  • Influence of the molecular environment on phosphorylated amino acid models: a density functional theory study.
  • The allosteric effect of fructose bisphosphate on muscle pyruvate kinase studied by infrared spectroscopy.
  • Effects of ions on ligand binding to pyruvate kinase: mapping the binding site with infrared spectroscopy.
  • Simulation of the amide I absorption of stacked β-sheets.
  • Quantifying bond distortions in transient enzyme species by a combination of density functional theory calculations and time-resolved infrared difference spectroscopy. Implications for the mechanism of dephosphorylation of the sarcoplasmic reticulum Ca2+-ATPase (SERCA1a)
  • 13C- and 15N-labeling of amyloid-β and inhibitory peptides to study their interaction via nanoscale infrared spectroscopy
  • The amyloid-inhibiting NCAM-PrP peptide targets Aβ peptide aggregation in membrane-mimetic environments
  • Abundance and composition of near surface microplastics and plastic debris in the Stockholm Archipelago, Baltic Sea
  • Pushing the detection limit of infrared spectroscopy for structural analysis of dilute protein samples
  • Simultaneous acquisition of infrared, fluorescence and light scattering spectra of proteins: direct evidence for pre-fibrillar species in amyloid fibril formation
  • Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets
  • Insight into the internal structure of amyloid-β oligomers by isotope-edited Fourier transform infrared spectroscopy
  • Correlations between the structure and the vibrational spectrum of the phosphate group. Implications for the analysis of an important functional group in phosphoproteins
  • The Amide I Spectrum of Proteins—Optimization of Transition Dipole Coupling Parameters Using Density Functional Theory Calculations
  • Correction to “The Amide I Spectrum of Proteins—Optimization of Transition Dipole Coupling Parameters Using Density Functional Theory Calculations”
  • Structure–Function Relationship of Artificial Spider Silk Fibers Produced by Straining Flow Spinning
  • On the Secondary Structure of Silk Fibroin Nanoparticles Obtained Using Ionic Liquids: An Infrared Spectroscopy Study
  • Direct Quantification by Infrared Spectroscopy of Drug Loading Content in Polymeric Nanoparticles
  • Direct Quantification of Drug Loading Content in Polymeric Nanoparticles by Infrared Spectroscopy
  • Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size
  • Analytical Time-Resolved Studies Using Photochemical Triggering Methods
  • Resolution of Trp near UV CD spectra of calmodulin-domain peptide complexes into the 1La and 1Lb component spectra
  • Fine-structure enhancement - assessment of a simple method to resolve overlapping bands in spectra
  • The study of protein reactions by reaction-induced infrared difference spectroscopy
  • ATP-induced phosphorylation of the sarcoplasmic reticulum Ca2+ ATPase: Molecular interpretation of infrared difference spectra
  • Photorelease of carboxylic acids from 1-acyl-7-nitroindolines in aqueous solution: Rapid and efficient photorelease of L-glutamate [4]
  • Side-chain protonation and mobility in the sarcoplasmic reticulum Ca 2+-ATPase: Implications for proton countertransport and Ca 2+ release
  • Structural changes of the sarcoplasmic reticulum Ca2+-ATPase upon nucleotide binding studied by Fourier transform infrared spectroscopy
  • Synthesis and characterisation of 13C and 15N isotopomers of a 1-acyl-7-nitroindoline
  • Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms
  • The infrared absorption of amino acid side chains
  • Structural dynamics of the Ca2+-ATPase studied by time-resolved infrared spectroscopy
  • Analysis of a putative voltage-gated prokaryotic potassium channel
  • Phosphoenzyme conversion of the sarcoplasmic reticulum Ca2+-ATPase. Molecular interpretation of infrared difference spectra
  • Direct measurement of enzyme activity with infrared spectroscopy
  • A dialysis accessory for attenuated total reflection infrared spectroscopy
  • Infrared spectroscopy - Past and present
  • P3-[2-(4-hydroxyphenyl)-2-oxo]ethyl ATP for the rapid activation of the Na+,K+-ATPase
  • Substrate binding and enzyme function investigated by infrared spectroscopy
  • Phosphoenolpyruvate and Mg2+ binding to pyruvate kinase monitored by infrared spectroscopy.
  • Following enzyme activity with infrared spectroscopy.
  • Influence of residue 22 on the folding, aggregation profile, and toxicity of the Alzheimer's amyloid beta peptide.
  • Structural changes in the catalytic cycle of the Na+,K+-ATPase studied by infrared spectroscopy.
  • Infrared spectrum of phosphoenol pyruvate: computational and experimental studies.
  • Photochemistry and thermal decarboxylation of alpha-phosphoryloxy-p-nitrophenylacetates.
  • Secondary structure transitions and aggregation induced in dynorphin neuropeptides by the detergent sodium dodecyl sulfate.
  • Time-resolved infrared spectroscopy of pH-induced aggregation of the Alzheimer Abeta(1-28) peptide.
  • Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.
  • Studies of decarboxylation in photolysis of alpha-carboxy-2-nitrobenzyl (CNB) caged compounds.
  • Proton paths in the sarcoplasmic reticulum Ca(2+) -ATPase.
  • Infrared spectroscopy of proteins.
  • Structures of the Ca2+-ATPase complexes with ATP, AMPPCP and AMPPNP. An FTIR study.
  • Toward a general method to observe the phosphate groups of phosphoenzymes with infrared spectroscopy.
  • Inhibition and partial reactions of Na,K-ATPase studied by Fourier transform infrared difference spectroscopy.
  • FTIR studies on the bond properties of the aspartyl phosphate moiety of the Ca2+ -ATPase.
  • Decarboxylation is a significant reaction pathway for photolabile calcium chelators and related compounds.
  • Interactions of phosphate groups of ATP and Aspartyl phosphate with the sarcoplasmic reticulum Ca2+-ATPase: an FTIR study.
  • Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase.
  • Flash photolytic release of alcohols from photolabile carbamates or carbonates is rate-limited by decarboxylation of the photoproduct.
  • P-O bond destabilization accelerates phosphoenzyme hydrolysis of sarcoplasmic reticulum Ca2+ -ATPase.
  • Phosphorylation of the sarcoplasmic reticulum Ca(2+)-ATPase from ATP and ATP analogs studied by infrared spectroscopy.
  • TNP-AMP binding to the sarcoplasmic reticulum Ca(2+)-ATPase studied by infrared spectroscopy.
  • Light-induced changes in the chemical bond structure of light-harvesting complex II probed by FTIR spectroscopy.
  • Photolytic cleavage of 1-(2-nitrophenyl)ethyl ethers involves two parallel pathways and product release is rate-limited by decomposition of a common hemiacetal intermediate.
  • Mapping interactions between the Ca2+-ATPase and its substrate ATP with infrared spectroscopy.
  • Characterization of a new caged proton capable of inducing large pH jumps.
  • What vibrations tell us about proteins.
  • Selective monitoring of 3 out of 50,000 protein vibrations.
  • Mapping nucleotide binding site of calcium ATPase with IR spectroscopy: effects of ATP gamma-phosphate binding.
  • Preparation of active enzyme samples for IR studies of Na+/K+-ATPase.
  • Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase
  • Ca2+ release from the phosphorylated and the unphosphorylated sarcoplasmic reticulurn Ca2+ ATpase results in parallel structural changes. An infrared spectroscopic study
  • Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity. A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle
  • Changes of protein structure, nucleotide microenvironment, and Ca2+-binding states in the catalytic cycle of sarcoplasmic reticulum Ca2+-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy
  • Time-resolved infrared spectroscopy of the Ca2+-ATPase. The enzyme at work
  • Structural changes of sarcoplasmic reticulum Ca2+-ATPase upon Ca2+ binding studied by simultaneous measurement of infrared absorbance changes and changes of intrinsic protein fluorescence
  • Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence
  • Fourier transform infrared (FTIR) spectroscopic investigation of the nicotinic acetylcholine receptor (nAChR) Investigation of agonist binding and receptor conformational changes by flash-induced release of 'caged' carbamoylcholine
  • Time-resolved infrared spectroscopy of intermediates and products from photolysis of 1-(2-nitrophenyl)ethyl phosphates: Reaction of the 2- nitrosoacetophenone byproduct with thiols
  • Photochemical Release of ATP from “Caged ATP” Studied by Time-Resolved Infrared Spectroscopy
  • Force-Induced Structural Changes in Spider Silk Fibers Introduced by ATR-FTIR Spectroscopy
  • Refining protein amide I spectrum simulations with simple yet effective electrostatic models for local wavenumbers and dipole derivative magnitudes
  • Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers

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