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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