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BIOCHEMISTRY
 
 

Dr. Paul Carey

Professor

Pub Med:

Dr. Paul Carey

The underlying theme of the research in the Carey laboratory is to relate structure to function, with special emphasis being on achieving a precise understanding of enzyme catalysis.

One of the great achievements of 20th century biology is the determination and visualisation of macromolecular structures. For many of these, the next challenge is to find out how they work at the molecular level. The principal technique used is a laser light scattering method called Raman spectroscopy. This approach enables us to determine both structural and bonding information for substrates at active sites. Thus, for the first time, we can begin to quantitate the contributions of effects such as substrate strain, hydrogen bonding and active site electric fields to enzyme reactivity.

Recent improvements in spectrometer performance, developed in the Carey lab, have provided access to enzyme systems that have been difficult, or impossible, to study by Raman spectroscopy. These include enzymes containing flavins, such as parahydroxybenzoate hydroxylase, that were intractable due to fluorescence interference, and enzymes such as dehalogenase that were difficult to obtain at sufficient concentrations to perform Raman difference spectroscopy. With the novel sensitive instrumentation, dehalogenase, which removes chlorine from chlorinated hydrocarbons, is now yielding a plethora of Raman data in the 100 micromolar concentration range. The research is highly interdisciplinary and involves, for example, enzyme chemistry, protein engineering and spectroscopy. The group collaborates extensively with other researchers at Case Western and at other institutions.

More detailed description of the research projects.

Selected References