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  • Tribute to a Lifelong Innovator: John Markley and the Evolution of Biomolecular NMR

Tribute to a Lifelong Innovator: John Markley and the Evolution of Biomolecular NMR

Submission Deadline: December 31, 2025Contribute to this Special Topic

This special collection celebrates Professor John L. Markley for his contributions to the field of biological nuclear magnetic resonance spectroscopy. Professor Markley pioneered the use of stable isotope (2H, 13C, and 15N) labeling to simplify spectra and assist in the assignment of NMR signals. He demonstrated how NMR data could be used to identify protonation states of proteins and to follow coupled equilibria and define thermodynamic properties of biological macromolecules, including multiple conformational states. As an assistant professor, his studies were enabled by access to NIH-funded NMR instrumentation at Carnegie Mellon University. To pay this forward for the next generations of young investigators, Professor Markley founded the Purdue University Biological Magnetic Resonance Laboratory and subsequently the National Magnetic Resonance Facility at Madison. His laboratory carried out early studies of multinuclear NMR spectroscopy, in particular the use of low level 13C labeling and 13C detection of 1H-13C and 13C-13C interactions. He developed efficient recombinant DNA technology for producing stable isotope labeled proteins from cells and cell-free extracts. His group developed methods for determining the strengths of hydrogen bonds and the influence on hydrogen bonding on the redox potentials of metalloproteins. He helped elucidate enzyme mechanisms and the pathway of iron-sulfur cluster assembly. Professor Markley and his associates stressed the importance of archiving validated NMR parameters and founded the Biological Magnetic Resonance Data Bank (BMRB) and guided its development and affiliation with the Protein Data Bank. The Markley group developed and disseminated software tools for NMR parameter identification, assignment, and structure determination. The group carried out early studies of NMR-based metabolomics and developed freely accessible libraries of NMR parameters of metabolites.

We call for reviews, forward looking perspectives, and original articles influenced by or related to Professor Markley’s work.

Topics covered include, but are not limited to:

  • Protein structures and their dynamics
  • Protein production and labeling strategies
  • Protein conformational states and their rates of interconversion
  • Peptide sequence/structure
  • Molecular interactions
  • Enzyme mechanisms
  • Proteinases and their inhibitors
  • Metalloproteins
  • Iron sulfur proteins
  • Metabolomics
  • Hydrogen bonding
  • Unpaired electron distributions
  • Calculation of observable NMR parameters
  • Software for the analysis of biomolecular NMR data
  • Science funding: shared instrumentation facilities, data repositories

Guest Editors:
Milo Westler, University of Wisconsin-Madison

Eldon Ulrich, University of Wisconsin-Madison

Art Edison, University of Georgia

Submission Deadline: December 31, 2025Contribute to this Special Topic
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