Research in Biophysics: The Functional Importance of Protein Structures (Jane Dyson)

     Jane Dyson, PhD, is a biophysicist and professor of integrative structural and computational biology at the Scripps Research Institute in La Jolla, California. As an undergraduate, Dyson had already begun to demonstrate an interest in science and in 1973 received a bachelor's of science in biochemistry from the University of Sydney in Australia. She continued her studies at the University of Australia for graduate school and in 1977 received a PhD in inorganic chemistry. She later went on to complete a postdoctoral fellowship at Massachusetts Institute of Technology (MIT) in 1977. Towards the beginning of her career, Dyson also worked at MIT in the Department of Biology. Following her time in Boston, Dyson became a UNESCO Lecturer in the School of Chemistry at the University of New South Wales from 1979 to 1984. Professor Jane Dyson joined the lab of Richard Lerner at the Scripps Research Institute in 1984 and has spent the majority of her career at this institution. In 1992, she became an associate professor in the Department of Molecular Biology and in 2001 was promoted to professor. As a professor, Dyson is well known in the field of biophysics for her work on intrinsically disordered proteins. As of 2017, Dyson became the first woman editor-in-chief of the Biophysical Journal, a peer-reviewed scientific journal that publishes articles and studies pertaining to biophysical questions and research. 

    Although her educational and professorial background may suggest that her interests lie primarily in the fields of chemistry and biology, her research incorporates both disciplines of biology and physics to explain natural phenomenon, namely the structure and function of proteins. Using techniques of Nuclear Magnetic Resonance Spectroscopy (NMR), mass spectrometry, circular dichroism and fluorescence spectroscopy, Dyson and her research team analyze the structure of proteins and study the relationships between the amino acid sequences of proteins and their structure and function. NMR, however, is Dyson's primary method of choice in studying unfolded and highly disordered proteins. NMR spectroscopy is an analytical chemistry technique used on chemical samples to analyze molecular structure from numerous generated identifiable peaks corresponding to known compounds. 

    Dyson's research interests lie predominantly in understanding the nature and behavior of unfolded and disordered proteins. Many important proteins, in fact, contain disordered or highly dynamic regions and NMR is the best technique to study these proteins as other methods are unable to determine protein structure for more mobile or disordered proteins. However, NMR techniques can ably determine the structure of flexible portions of a protein and, therefore, provide accurate structural information for highly disordered or unfolded proteins. 

    As scientific databases listing the amino acid sequences of numerous proteins become populated with increasingly more entries, Dyson has noticed that several of these entries appear to code for proteins that should be intrinsically unstructured. Thus, unfolded or disordered proteins are not an uncommon occurrence in nature and Dyson is interested in how the mechanisms and function of these proteins compare to highly ordered proteins. She wants to better understand why these intrinsically disordered proteins are structured as they are and how their structure aids in their ability to perform necessary functions in the cell. 

    Dyson studies protein dynamics and is interested in how intra-protein movement and disorder affects protein function. To study these topics, she employs the concepts of physics to understand how and the extent to which the unfolded or disordered portions of a protein move. She looks at the degree of motion and flexibility within a protein and relates these observations to changes in function, since structure and function are closely related in proteins. Dyson, therefore, uses physics to study how the protein moves and how that flexibility affects the rest of the protein and then, from a biological stand point, looks at how the dynamic nature of a disordered protein influences its function and its ability to interact with other species. 

    Specifically, Dyson's research has focused on studying the interaction of the transcription factor NF-kappaB complexes with DNA and its inhibitor IkappaB. NF-kappaB is a protein complex that controls DNA transcription, cytokine production and cell survival and Dyson's research has lead to novel insights into the mechanisms by which NF-kappaB transcriptional activation is turned on and off. Her other emphasis is on the interactions of chaperones with co-chaperones and with proteins whose folding and unfolding they assist.