Peter Wright is a Professor in the Department of Integrative Structural and Computational Biology and holds the Cecil H. and Ida M. Green Chair of Biomedical Research at The Scripps Research Institute. He received B.Sc., M.Sc. and Ph.D. degrees from the University of Auckland, New Zealand, and undertook postdoctoral studies at Oxford University, UK. He joined the faculty at the University of Sydney, Australia in 1976. He was appointed to the faculty of Scripps in 1984 as Professor and was Chair of the Department of Molecular Biology from 1987-2012. His research has focused on applications of nuclear magnetic resonance to study mechanisms of protein folding and misfolding, the structural basis of protein-protein and protein-nucleic acid interactions in the regulation of gene expression, and the role of dynamics in protein function. His work on protein interactions led to the realization that many proteins are intrinsically disordered, and that protein disorder plays an important functional role in cellular signaling networks. He is an elected fellow of the International Society of Magnetic Resonance, the NMR Society of Japan, the American Association for the Advancement of Science, and the American Academy of Arts and Sciences. He is Editor-in-Chief of the Journal of Molecular Biology.

Research Interests

My laboratory utilizes high-resolution NMR spectroscopy and other biophysical methods to investigate the structure, dynamics, and folding/misfolding mechanisms of proteins and to map their functional interactions. NMR is unique as a method for determining three-dimensional structures of proteins and protein complexes in solution and providing novel information about their time-dependent structural fluctuations that are essential for protein function. We are using a multidisciplinary approach to map the structural ensembles, dynamics, and functional interactions of intrinsically disordered proteins of central importance in regulation of eukaryotic cells. These proteins include key transcriptional coactivators and transcription factors, such as the tumor suppressor p53, as well as intrinsically disordered viral proteins that target critical host cell proteins to dysregulate cellular signaling processes. We are also applying powerful NMR methods to study the fundamental molecular pathways by which proteins misfold and aggregate to cause human disease. Our current research is focused on the protein transthyretin and the mechanism by which the transthyretin tetramer dissociates and unfolds to form aggregation-prone intermediates that are associated with neurodegenerative disease and cardiomyopathies.

Membership Type


Election Year


Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 21: Biochemistry