Juliette Lecomte

Dr. Juliette Lecomte is a Professor in the Department of Biophysics at Johns Hopkins University, where she has been since 2007. Previously, she served on the Chemistry faculty at The Pennsylvania State University from 1987 to 2007, advancing from Assistant to Associate to Professor. Her research is centered in experimental biophysical chemistry, with a focus on protein structure and dynamics in solution.

• Ph.D. in Chemistry, Carnegie-Mellon University (1982)
• M.S. in Chemistry, Carnegie-Mellon University
• Licence en Sciences Chimiques, Université de Liège, Belgium
• Postdoctoral Research, University of California, Davis

Her research explores the stability, structure, and dynamics of proteins, particularly heme proteins such as hemoglobins and cytochromes. She investigates protein-cofactor recognition and allosteric effects using nuclear magnetic resonance (NMR) spectroscopy and optical spectroscopy as primary tools. Her work provides deep insights into the functional mechanisms of metalloproteins in biological systems.

The analysis of her recent publications shows a consistent focus on cyanobacterial hemoglobins, apoproteins, and photosystem components. Her studies often involve detailed NMR characterization of protein conformations, dynamics, and ligand interactions. Keywords across her work include protein folding, heme binding, covalent modifications, and structural homology.

She has mentored numerous graduate students and postdoctoral researchers, many of whom are listed as former lab members. Her lab has been active for decades, contributing significantly to the field of biophysical chemistry.

• Structural and dynamic studies of heme proteins
• NMR-based protein characterization
• Protein-cofactor interactions
• Allosteric regulation in globins
• Solution-state biophysics

Dr. Lecomte leads an active research group within the Department of Biophysics and the Program in Molecular Biophysics at Johns Hopkins University. Her lab, located in Jenkins Hall, utilizes advanced NMR instrumentation and spectroscopic methods to probe protein behavior in solution. The group has produced a substantial body of work, particularly on cyanobacterial model systems, and continues to explore fundamental questions in protein science.