报告主题：Mass spectrometry - from folding proteins to rotating motors
Dr Lee's Professor of Chemistry, University of Oxford
President Elect, Royal Society of Chemistry
Dame Commander of the Order of the British Empire
Carol Robinson holds the Chair of Dr. Lee’s Professor of Chemistry at theUniversity of Oxford. She is recognized for using mass spectrometry to furtherresearch into the 3D structure of proteins and their complexes. Carol’sresearch has attracted international awards and prizes including the AnfinsenAward from the Protein Society, the Biemann Medal from the American Society ofMass Spectrometry, the Davy Medal and the Rosalind Franklin Award from theRoyal Society, the HUPO Award for Distinguished Achievement, the Anatrace Awardfrom the American Biophysical Society, the Kaj Lindström-Lang Prize from theCarlsberg Research Center and the Torbern Bergmann Award from the SwedishChemical Society.
Two decades after the introduction of electrospray for the analysis ofproteins the mass spectra of intact ribosomes have become almost routine. These2.5 MDa particles remain intact during their flight through the massspectrometer yielding new information about the stoichiometry of subcomplexesand the effects of modifications. However, knowledge of the intact mass of aprotein or complex is only one part of the mass spectrometry informationavailable. Data from the disruption of protein complexes is leadingto subunit interaction maps and architectural models. Such models are enhancedby coupling with ion mobility mass spectrometryin which the collisioncross-section of a protein complex can be defined. With theadvent of massspectra of membrane embedded macromolecular complexesnew information and hypothesesare emerging about the effects of lipid binding. Human exploration of theprotein has been a long way, in this, and life is closely related to theprotein is gradually faded its mysterious and beautiful and unpredictable coat.In this lecture, we will follow Carol Robinson's pace, together to trace thiswonderful journey.