Daniel A. Rutz

ORCID: 0000-0001-9997-7468
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About
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Research Areas
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Computational Drug Discovery Methods
  • Advanced Battery Technologies Research
  • Toxin Mechanisms and Immunotoxins
  • Advancements in Battery Materials
  • thermodynamics and calorimetric analyses
  • Advanced Electron Microscopy Techniques and Applications
  • Plant biochemistry and biosynthesis
  • Extraction and Separation Processes
  • Ion-surface interactions and analysis
  • RNA and protein synthesis mechanisms
  • Genetics, Aging, and Longevity in Model Organisms
  • Electrical and Bioimpedance Tomography

Technical University of Munich
2013-2022

Center for Integrated Protein Science Munich
2014-2022

Universität Ulm
2022

Roche Pharma AG (Germany)
2021

Abstract The heat shock protein 90 (Hsp90) is a molecular chaperone that employs the free energy of ATP hydrolysis to control folding and activation several client proteins in eukaryotic cell. To elucidate how local ATPase reaction active site couples global conformational dynamics Hsp90, we integrate here large-scale simulations with biophysical experiments. We show switching conserved ion pairs between N-terminal domain, harbouring site, middle domain strongly modulates catalytic barrier...

10.1038/s41467-020-15050-0 article EN cc-by Nature Communications 2020-03-16

Hsp90 is a molecular chaperone that interacts with specific set of client proteins and assists their folding. The underlying mechanisms, involving dynamic transitions between open closed conformations, are still enigmatic. Combining nuclear magnetic resonance, small-angle x-ray scattering, biochemical experiments, we have identified key intermediate state induced by adenosine triphosphate (ATP) binding, in which rotation the N-terminal domain (NTD) yields arrangement poised for closing. This...

10.1126/sciadv.abl7295 article EN cc-by-nc Science Advances 2021-12-17

Abstract Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for middle-domain (Hsp90-M) scarce. Here we report on tryptophan residue Hsp90-M as new type point. Our study shows this conserved senses interaction Hsp90 with stringent client transfers via cation–π neighboring...

10.1038/s41467-018-03946-x article EN cc-by Nature Communications 2018-04-11

Abstract Protein phosphatase 5 is involved in the regulation of kinases and transcription factors. The dephosphorylation activity modulated by molecular chaperone Hsp90, which binds to TPR-domain protein 5. This interaction dependent on C-terminal MEEVD motif Hsp90. We show that Hsp90 fragments differ their hinting a more complex interaction. Also hydrodynamic parameters from analytical ultracentrifugation small-angle X-ray scattering data suggest compact structure for Hsp90-protein...

10.1038/srep17058 article EN cc-by Scientific Reports 2015-11-23

Heat shock protein 90 (Hsp90) is a highly conserved ATP-driven machine involved in client maturation, folding, and activation. The chaperone supported by set of cochaperones that confer specificities. One those proteins the suppressor G2 allele skp1 (Sgt1), which participates together with Hsp90 immune responses plants. Sgt1 consists three domains: TPR-, CS-, SGS-domain, plants, yeast, humans. TPR-domain though lacking nematodes insects. We observe Caenorhabditis elegans homologue D1054.3...

10.1021/bi5000542 article EN Biochemistry 2014-03-24

Reference electrodes (REs) are powerful tools to analyze electrochemical phenomena within lithium ion batteries. However, their design and material choice under debate. Recently, titanate oxide (LTO, Li4Ti5O12) iron (LFP, LiFePO4) have been dip-coated onto wide-meshed metal nets reduce the blocking effect. Still, this process is elaborate not common in electrode manufacturing.In study, we show a post-processing method fabricate user-defined REs based on LFP via an ultrashort pulse laser. The...

10.2139/ssrn.4186806 article EN SSRN Electronic Journal 2022-01-01

The implementation of reference electrodes (RE) in lithium-ion battery cells represents a promising way to optimize fast-charging, evaluate the C-rate capability new electrode materials, and monitor cell aging more precisely. However, their design material choice are under debate. Recently, lithium titanate oxide (LTO, Li 4 Ti 5 O 12 ) iron (LFP, LiFePO have been dip-coated onto wide-meshed metal nets reduce blocking effect. Still, this process is elaborate not common manufacturing. In...

10.1149/ma2022-0272444mtgabs article EN Meeting abstracts/Meeting abstracts (Electrochemical Society. CD-ROM) 2022-10-09
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