Electrospray ionization (ESI) is a technique used in mass spectrometry to produce ions using an electrospray in which a high voltage is applied to a liquid to create an aerosol. It is especially useful in producing ions from macromolecules because it overcomes the propensity of these molecules to fragment when ionized. ESI is different from other ionization processes since it may produce multiple-charged ions, effectively extending the mass range of the analyser to accommodate the kDa-MDa orders of magnitude observed in proteins and their associated polypeptide fragments.
Richard Chace Tolman was an American mathematical physicist and physical chemist who made many contributions to statistical mechanics. He also made important contributions to theoretical cosmology in the years soon after Einstein's discovery of general relativity. He was a professor of physical chemistry and mathematical physics at the California Institute of Technology (Caltech).
Electron-capture dissociation (ECD) is a method of fragmenting gas-phase ions for structure elucidation of peptides and proteins in tandem mass spectrometry. It is one of the most widely used techniques for activation and dissociation of mass selected precursor ion in MS/MS. It involves the direct introduction of low-energy electrons to trapped gas-phase ions.
Electron-transfer dissociation (ETD) is a method of fragmenting multiply-charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry (MS/MS). Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them. ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis. Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving labile post translational modifications (PTM) intact. The technique only works well for higher charge state peptide or polymer ions (z>2). However, relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins. This makes the technique important for top-down proteomics. The method was developed by Hunt and coworkers at the University of Virginia.
Fred Warren McLafferty was an American chemist known for his work in mass spectrometry. He is best known for the McLafferty rearrangement reaction that was observed with mass spectrometry. With Roland Gohlke, he pioneered the technique of gas chromatography–mass spectrometry. He is also known for electron-capture dissociation, a method of fragmenting gas-phase ions.
David E. Clemmer is an analytical chemist and the Distinguished Professor and Robert and Marjorie Mann Chair of Chemistry at Indiana University in Bloomington, Indiana, where he leads the Clemmer Group. Clemmer develops new scientific instruments for ion mobility mass spectrometry (IMS/MS), including the first instrument for nested ion-mobility time-of-flight mass spectrometry. He has received a number of awards, including the Biemann Medal in 2006 "for his pioneering contributions to the integration of ion mobility separations with a variety of mass spectrometry technologies."
Dame Carol Vivien Robinson, is a British chemist and former President of the Royal Society of Chemistry (2018–2020). She was a Royal Society Research Professor and is the Dr Lee's Professor of Physical and Theoretical Chemistry, and a Professorial Fellow at Exeter College, University of Oxford. She is the first director of the Kavli Institution for Nanoscience Discovery, University of Oxford, and she was previously Professor of Mass Spectrometry at the Department of Chemistry of the University of Cambridge.
Kevin Downard is a British - Australian academic scientist whose research specialises in the improving responses to infectious disease through the application and development of mass spectrometry and other molecular approaches in the life and medical sciences. Downard has over 35 years of experience in the field and has written over 140 lead-author scientific peer-reviewed journal publications, and two books including a textbook for the Royal Society of Chemistry and the first book to be published on the role of mass spectrometry in the study of protein interactions.
Renato Zenobi is a Swiss chemist. He is Professor of Chemistry at ETH Zurich. Throughout his career, Zenobi has contributed to the field of analytical chemistry.
Albert J.R. Heck is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He is known for his work on technologies to study proteins in their natural environment, with the aim to understand their biological function. Albert Heck was awarded the Spinoza Prize in 2017, the highest scientific award in the Netherlands.
Natalie G. Ahn is a professor of chemistry and biochemistry at the University of Colorado at Boulder. Her research is focused on understanding the mechanisms of cell signaling, with a speciality in phosphorylation and cancers. Ahn's work uses the tools of "classical chemistry" to work on understanding the genetic code and how genetics affects life processes. She has been a professor at the University of Colorado at Boulder since 2003, where she is a Distinguished Professor. She was a Howard Hughes Medical Institute investigator between 1994 and 2014. In 2018, she was elected to the National Academy of Sciences and named a fellow of the American Academy of Arts and Sciences.
Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. Radford is the Associate Editor of the Journal of Molecular Biology.
Margaret Mary Sheil is an Australian academic and the Vice Chancellor and President of Queensland University of Technology.
Ancient proteins are complex mixtures and the term palaeoproteomics is used to characterise the study of proteomes in the past. Ancients proteins have been recovered from a wide range of archaeological materials, including bones, teeth, eggshells, leathers, parchments, ceramics, painting binders and well-preserved soft tissues like gut intestines. These preserved proteins have provided valuable information about taxonomic identification, evolution history (phylogeny), diet, health, disease, technology and social dynamics in the past.
Katerina Douka is an archaeological scientist whose work focuses on the spatio-temporal pattern of human dispersals and extinctions across Eurasia, including Neanderthals, Denisovans and modern Homo sapiens.
Camilla F. Speller is a biomolecular archaeologist, Assistant Professor in Anthropological Archaeology at the University of British Columbia Department of Anthropology.
Claire Eyers is a British biological mass spectrometrist who is professor of biological mass spectrometry at the University of Liverpool, where she heads up the Centre for Proteome Research. Her research publications list her either as Claire E Haydon or Claire E Eyers.
Zooarchaeology by mass spectrometry, commonly referred to by the abbreviation ZooMS, is a scientific method that identifies animal species by means of characteristic peptide sequences in the protein collagen. ZooMS is the most common archaeological application of peptide mass fingerprinting (PMF) and can be used for species identification of bones, teeth, skin and antler. It is commonly used to identify objects that cannot be identified morphologically. In an archaeological context this usually means that the object is too fragmented or that it has been shaped into an artefact. Archaeologists use these species identification to study among others past environments, diet and raw material selection for the production of tools.
Richard M. Caprioli is an American chemist known for his contributions to mass spectrometry imaging.
Alison E Ashcroft is a British chemist and Emeritus Professor of Biomolecular Mass Spectrometry at the University of Leeds. Her work is focused on method development in mass spectrometry to study protein folding and protein aggregation in relation to diseases.
