Novel synthetic chemistry of ureas and amides

In this thesis, the author investigates the chemistry and application of molecules containing urea and amide bonds. These bonds are some of the strongest known and are fundamental to biological processes. The author describes his discovery that sterically hindered ureas undergo solvolysis at room te...

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Xehetasun bibliografikoak
Egile nagusia: Hutchby, Marc, 19..-
Formatua: Livre numérique
Hizkuntza:Anglais
Argitaratua: Berlin, Heidelberg : Springer Berlin Heidelberg [20..].
Cham : Springer Nature
Edizioa:1st ed. 2013.
Saila:Springer Theses, Recognizing Outstanding Ph.D. Research
Sarrera elektronikoa:Accès sur la plateforme de l'éditeur
Accès sur la plateforme Istex
Accès Université d'Orléans
Accès INSA CVL
Oharra: Archives Springer e-books (Licence nationale)
Archives Springer e-books (Licence nationale)
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Edition sous un autre format:• Novel Synthetic Chemistry of Ureas and Amides, Texte imprimé, 9783642320507
• Novel Synthetic Chemistry of Ureas and Amides, Texte imprimé, 9783642448904
• Novel Synthetic Chemistry of Ureas and Amides, Texte imprimé, 9783642320521
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505 1 |a Transition metal catalysis Palladium catalysis Pd(II) catalysed aminocarbonylation of alkenes Carbonylation of aryl ureas Urea Hydrolysis Amide hydrolysis 
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520 |a In this thesis, the author investigates the chemistry and application of molecules containing urea and amide bonds. These bonds are some of the strongest known and are fundamental to biological processes. The author describes his discovery that sterically hindered ureas undergo solvolysis at room temperature under neutral conditions. This is a remarkable finding, since ureas are inert under these conditions and a general rule of chemistry is that hindered substrates are less reactive. Remarkably, the author translates these results to the correspondingly sterically hindered amides. This thesis has resulted in a number of outstanding publications in high profile journals. The unique method for breaking urea and amide bonds developed in this study is likely to have far reaching consequences for biological protein manipulation 
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