Carol Robinson
University of Oxford, United Kingdom
From Peripheral Proteins to Membrane Motors – Mass Spectrometry Comes of Age
Monday, March 4, 8:00 PM
Baltimore Convention Center
Being named the 2019 Biophysical Society Lecturer is the highest annual award bestowed by the Biophysical Society. In addition to presenting the Annual Biophysical Society Lecture, the recipient provides a molecule or figure that depicts his/her research. That figure is used in the background design for that year’s Annual Meeting print and web announcements.
Professor Robinson holds the Chair of Doctor Lee’s Professor of Chemistry at the University of Oxford. She is renowned for pioneering the use of mass spectrometry for her ground-breaking research into the 3D structure of proteins.
Carol was a graduate student at Churchill College from 1980 -1982, completing her PhD in two years. Following an eight-year career break to begin raising her three children, she returned to research at Oxford, later becoming a titular professor in 1999.
In 2001 she returned to Cambridge to continue her research into mass spectrometry and was elected a Professorial Fellow at Churchill College, a Fellow of the Royal Society in 2004, and a Royal Society Research Professor in 2006. In 2009 she was elected Doctor Lee’s Professor of Chemistry at the University of Oxford and in 2013 was awarded the title of Dame Commander of the Order of the British Empire.
The Image: Lipid Connections Caught in the Gas Phase of a Mass Spectrometer
Protein subunits of LeuT (PDB ID 2A65 green, purple) form a lipid-mediated dimer in the presence of cardiolipin (red head-group, grey side-chain). The quadrupole rods (silver) enable the discovery of lipid binding to membrane proteins through tandem mass spectrometry experiements.