Maxim A. Droemer

ORCID: 0009-0009-5280-2041
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About
Contact & Profiles
Research Areas
  • Protein Structure and Dynamics
  • Advanced NMR Techniques and Applications
  • NMR spectroscopy and applications
  • Bacterial biofilms and quorum sensing
  • Antibiotic Resistance in Bacteria
  • Metabolomics and Mass Spectrometry Studies
  • Enzyme Structure and Function
  • Endoplasmic Reticulum Stress and Disease
  • Antimicrobial Peptides and Activities

Ludwig-Maximilians-Universität München
2024-2025

Dana-Farber Cancer Institute
2023

Harvard University
2023

ATP analogues are essential tools in enzymology and structural biology, but the functional implications of their chemical modifications on nucleotide-binding proteins often underappreciated. To address this, we evaluated a panel analogues, focusing thiosubstituted fluorinated molecules, using AAA+ ATPase p97 as benchmark system. Hydrolysis stability impact protein conformation, binding modes, kinetics enzymatic catalysis were assessed by protein-detected methyl NMR ligand-detected 19F...

10.3390/biophysica5010009 article EN cc-by Biophysica 2025-03-10

The current standard method for amino acid signal identification in protein NMR spectra is sequential assignment using triple-resonance experiments. Good software and elaborate heuristics exist, but the process remains laboriously manual. Machine learning does help, its training databases need millions of samples that cover all relevant physics every kind instrumental artifact. In this communication, we offer a solution to problem. We propose polyadic decompositions store simulated...

10.1126/sciadv.ado0403 article EN cc-by-nc Science Advances 2024-09-04
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