Stanford University
Showing 961-980 of 5,807 Results
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Margaret Cohen
Andrew B. Hammond Professor of French Language, Literature, and Civilization and Professor, by courtesy, of French and Italian and of Comparative Literature
Current Research and Scholarly InterestsProfessor Cohen has devoted her career to the literature and culture of modernity. Her books include Profane Illumination (1993) on the impact of surrealist Paris on Walter Benjamin; The Sentimental Education of the Novel (1999), on the role of women writers in shaping 19th-century French realism; and The Novel and the Sea (2010), about how writings about work at sea shaped the adventure novel. Her forthcoming book explores how underwater film and TV have shaped the cultural imagination.
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Catherine Nicole Coleman
Research Director, Humanities+Design, Center for Interdisciplinary Digital Research
Affiliate, ClassicsBioNicole is Digital Research Architect for the Stanford University Libraries and Research Director for Humanities+Design, a research lab at the Center for Spatial and Textual Analysis. Nicole works at the intersection of the digital library and digital scholarship as a lead architect in the design and development of practical research services. She is currently leading an initiative within the Library to identify and enact applications of artificial intelligence —machine perception, machine learning, machine reasoning, and language recognition— to make the collections of maps, photographs, manuscripts, data sets and other assets more easily discoverable, accessible, and analyzable.
At Humanities + Design she has led the design and development of numerous tools for data visualization and analysis including Palladio, Breve, and Data Pen. The lab encourages and supports collaboration between researchers from the humanities and design to encode interpretive method in tools for data analysis. Lessons learned in that work have proven essential to improving the design of machine learning based tools for research. -
James Collman
George A. and Hilda M. Daubert Professor of Chemistry, Emeritus
BioProfessor Emeritus James Collman has made landmark contributions to inorganic chemistry, metal ion biochemistry, homogeneous catalysis, and transition metal organometallic chemistry. He pioneered numerous now-popular research tools to reveal key structural and functional details of metalloenzymes essential to respiration and energy, and hemoglobin and myoglobin, essential to oxygen transport in the blood.
Born 1932 in Beatrice, Nebraska, James P. Collman studied chemistry at U. Nebraska–Lincoln (B.S. 1954, M.S. 1956). His doctoral work at U. Illinois at Urbana-Champaign (Ph.D., 1958) focused on Grignard reagents. As a faculty member at U. North Carolina, he demonstrated aromatic reactivity in metal acetylacetonates, and he developed metal complexes that hydrolyze peptide bonds under physiological conditions. He came to Stanford University as Professor of Chemistry in 1967. Among many honors, Prof. Collman’s was elected to the National academy of Sciences in 1975, and named California Scientist of the Year in 1983.
At Stanford, Prof. Collman invented a new paradigm for studying biological systems using functional synthetic analogs of metal-containing enzyme systems, free from the protein coatings that can affect metalloprotein chemical properties. This strategy allowed him to elucidate the intrinsic reactivity of the metal center as well as the effects of protein-metal interactions on biological function.
One focal point of this research has involved heme-proteins such as the oxygen (O2) carrier hemoglobin (Hb), and the O2-storing protein myoglobin (Mb). Prof. Collman was the first to prepare and characterize stable, functional analogues of the Hb and Mb active sites, which contain an iron derivative of the large flat “porphyrin” ligand. In his “picket fence” porphyrin, groups installed on the periphery block side reactions, which would otherwise degrade the structure. This protected iron complex manifests the unique magnetic, spectroscopic and structural characteristics of the O2-binding Hb and Mb sites, and exhibits very similar O2-binding affinities.
The Collman Group also prepared functional mimics of the O2-binding/reducing site in a key respiration enzyme, cytochrome c oxidase, CcO, which converts O2 to H2O during biosynthesis of the energy storage molecule ATP. This enzyme must be very selective: partial O2 reduction products are toxic. Prof. Collman invented a powerful synthetic strategy to create analogs of the CcO active site and applied novel electrochemical techniques to demonstrate that these models catalyze the reduction of O2 to water without producing toxic partially-reduced species. He was able to mimic slow, rate-limiting electron delivery by attaching his CcO model to a liquid-crystalline membrane using “click chemistry.” He demonstrated that hydrogen sulfide molecules and heterocycles reversibly bind to the metal centers at CcO’s active site, connecting a synthetic enzyme model to simple molecules that reversibly inhibit respiration. These respiration inhibitors exhibit physiological properties, affecting blood clotting and controlling the effects of the hormone, nitric oxide, NO.
In addition, Prof. Collman performed fundamental studies of organometallic reactions. He also prepared and characterized homodinuclear and heterodinuclear complexes having metal-metal multiple bonds, and made the first measurements of the rotational barriers found in multiple metal-metal bonds.
Prof. Collman’s impactful textbook “Principles and Applications of Organotransition Metal Chemistry” has seen multiple editions. His book “Naturally Dangerous: Surprising Facts About Food, Health, and the Environment” explains the science behind everyday life, and received favorable reviews in Nature and The Washington Post.
