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Participants/Project Abstracts

Summer 2007 Bioanalytical Science REU Participants

Christine Reder

Christine E. Reder, Jolene K. Diedrich, Ryan R. Julian
Department of Chemistry, University of California – Riverside, UCR 92521 and Ferris State University, Big Rapids, MI 49307.


The focus of this project is to continue the development of the SNAPP technique, which can be used to observe protein structure using mass spectrometry.  Previous work with 18-crown-6 ether (18C6) has shown protein structure can be examined through the availability of amino acid side-chains, determined through the interaction of lysine and 18C6.  Here, the availability of arginine side-chains is explored though interactions with other crown ethers, as analyzed through the use of electrospray ionization mass spectrometry (ESI-MS).  Both, dibenzo-30-crown-10 ether (DB30C10) and DP (a crown ether which contains two endocyclic dialkylhydrogenphosphate esters) preferentially form noncovalent complexes with the guanidinium group of the arginine side-chain.  Experiments were conducted using various solvent conditions for each crown with ubiquitin.  Also, varying electrospray parameters were used for the ESI-MS analysis of ubiquitin and 18C6 solutions to observe the effects of the different settings on crown attachment.  DB30C10 shows a significant solvent effect on crown attachment with the addition of organic co-solvent to the solution.  DP binds to protein with an uneven distribution of crown among the charge states.  The 18C6 solutions illustrate the importance of keeping instrument settings constant through the course of an experiment because changes in the settings affect the number of crowns attaching.


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