John L. Markley

Photo of John L. Markley
Emeritus Professor 2020-present
Professor 1984-2020
Steenbock Professor of Biomolecular Structure
Emeritus Head of NMRFAM and BMRB
B.A., Carleton College
Ph.D., Harvard University
NIH Postdoctoral Fellow, University of California, Berkeley

NMR spectroscopy and its applications to protein structure and function and metabolomics

The primary focus of our research is on the structure and function of proteins. We have an NIH-funded project on the protein machinery involved in the biosynthesis and delivery of iron-sulfur clusters. We rely on NMR spectroscopy as a major approach to studying protein structure and dynamics and supplement this with information from small angle x-ray scattering (SAXS), differential scanning calorimetry (DSC), optical spectroscopy, and other biophysical approaches. At the National Magnetic Resonance Facility at Madison (NMRFAM,, we develop technology as driven by collaborative investigations on improved methods for collecting and analyzing NMR data from larger macromolecules and their complexes, biological fluids, cell extracts, and natural products. At the BioMagResBank (BMRB,, we maintain the primary depository for biomolecular NMR data. We strive to improve methods for depositing the growing range of data created by biomolecular NMR, and we work with the NMR community in developing better ways of validating the data and making it available in more meaningful ways. In the case of NMR-derived three three-dimensional structures, we partner with the Worldwide Protein Data Bank ( in creating depositions to the Protein Data Bank.


Example of an integrative/hybrid structural model

Example of an integrative/hybrid structural model of a complex of five human mitochondrial proteins derived from a combination of chemical crosslinking coupled with coupled with tandem mass spectrometry, small-angle X-ray scattering, NMR spectroscopy, and X-ray crystallography. Acp is acyl carrier protein, ISD11 is a small “LYRM” protein, FXN is ferredoxin, ISCU is the scaffold for iron-sulfur cluster assembly, and NFS1 is cysteine desulfurase. From Structure 26, 1127-1136 (2018).