Investigating the structure and dynamics of biological systems and complex formulations in the solid-state using NMR spectroscopy

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for investigating the structure and dynamics of biological systems and complex formulations in the solid state. This technique offers detailed insights into molecular interactions and structural properties, enhancing our understanding of various scientific processes. Here some examples from the field.

Exploring the function and malfunction of proteins in health & disease

Andrew Baldwin is a Professor of Physical and Theoretical Chemistry at the University of Oxford. His research focuses on using advanced biomolecular NMR techniques to study protein structure and dynamics, particularly in the context of protein misfolding diseases like Alzheimer's and Parkinson's.

Andrew Baldwin, professor of Physical and Theoretical Chemistry at the University of Oxford

Understanding different molecular mechanisms of lipid trafficking in pulmonary surfactant with NMR

Joanna Long is a professor of biochemistry and molecular biology at the University of Florida and an Associate Director of the U.S. National High Magnetic Field Laboratory. Her research group develops dynamic nuclear polarization for biological applications and uses high resolution and solid-state NMR spectroscopy to study the molecular underpinnings of biofilm formation and pulmonary surfactant properties.

Joanna Long, professor of biochemistry and molecular biology at the University of Florida and an Associate Director of the U.S. National High Magnetic Field Laboratory

Structural Studies of Disordered Proteins with NMR

Julie Forman-Kay delves into her research on intrinsically disordered proteins, which lack stable structures but play crucial roles in biology. Using advanced NMR techniques, her team studies these proteins’ dynamic ensembles and their behavior in biomolecular condensates. This research is pivotal for understanding how mutations in disordered regions contribute to diseases like autism spectrum disorder. Julie’s work highlights the importance of structural biology in uncovering the mechanisms behind protein function and pathology.

Julie Forman-Kay, Head of Molecular Medicine Program at the hospital for sick children Research Institute, Professor of Biochemistry, University of Toronto

Exploring the molecular world of proteins

Tatyana Polenova is a Professor of Chemistry and Biochemistry at the University of Delaware and leads a team of scientists at the Polenova Laboratory. Her research focuses on investigating the structure and dynamics of biological systems and complex formulations in the solid-state using NMR spectroscopy, combined with computational, and biochemical methods. Alongside her team at the Polenova Laboratory, she is currently studying HIV-1 capsid and SARS-CoV-2 protein assemblies, microtubule- and actin- associated protein assemblies, and vanadium-containing halo peroxidases, with the aim of better understanding disease mechanisms and assisting with drug discovery and development, as well as biotechnology applications.

Tatyana Polenova, Professor of Chemistry and Biochemistry at the University of Delaware, USA