G
George M. Whitesides
Researcher at Harvard University
Publications - 1754
Citations - 287794
George M. Whitesides is an academic researcher from Harvard University. The author has contributed to research in topics: Monolayer & Self-assembled monolayer. The author has an hindex of 240, co-authored 1739 publications receiving 269833 citations. Previous affiliations of George M. Whitesides include University of California, Davis & University of Texas at Austin.
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Journal ArticleDOI
Autocatalytic, bistable, oscillatory networks of biologically relevant organic reactions
Sergey Semenov,Lewis J. Kraft,Alar Ainla,Mengxia Zhao,Mostafa Baghbanzadeh,Victoria Campbell,Kyungtae Kang,Jerome M. Fox,George M. Whitesides,George M. Whitesides +9 more
TL;DR: By using small organic molecules to build a network of organic reactions with autocatalytic, bistable and oscillatory behaviour, principles are identified that explain the ways in which dynamic networks relevant to life could have developed.
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Thermal decomposition of vinylic copper(I) and silver(I) organometallic compounds
TL;DR: In this paper, it was shown that free propenyl radicais are not intermediates in these thermal coupling re-ttctions, when interpreted in light of the known rate of inversion of configuration of vinylradicirls.
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Structure-Reactivity Relations for Thiol-Disulfide Interchange
TL;DR: In this article, equilibrium constants were determined for thiol-disulfide interchange between 36 di- and trithiols and the disulfides derived from either 2-mercaptoethanol or dithiothreitol.
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Lipase-catalyzed hydrolysis as a route to esters of chiral epoxy alcohols
TL;DR: In this paper, a survey of enzymes that hydrolyze glycidol esters indicated that E.C. 3.1.3, Sigma Type II, from porcine pancreas, has the best combination of activi ty, select ivi ty and cost.
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Noncovalent Polycationic Coatings for Capillaries in Capillary Electrophoresis of Proteins
TL;DR: This study demonstrates that the charge ladder obtained by acetylation of lysozyme is a good model with which to test the efficiency of polycationic coatings, and suggests that protein adsorption is mainly driven by electrostatic interactions.