ANYL 328 |
| One of the lowest energy spontaneous decomposition processes of proteins is the deamidation of asparagine, and therefore this process is believed to be a principal contributor to the aging process. We have begun an examination of the energetics of this process and related decompositions by aspartic acid, glutamine, and glutamic acid by using model gas phase systems. Here both protonated and metallated amino acids are examined by collision induced dissociation in a guided ion beam mass spectrometer that is capable of determining the energetics of decomposition. Deamidation and dehydration processes compete with loss of the intact amino acid in the metallated cases, allowing a determination of the binding energetics to the amino acid and its fragment. Comparison with theory provides structural information that augments the experimental thermochemistry. The protonated species have more complex dissociation pathways that provide additional insight into these low energy decomposition pathways. |
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Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry in Honor of Jean H. Futrell
8:30 AM-12:20 PM, Tuesday, August 21, 2007 BCEC -- 104B, Oral
Division of Analytical Chemistry |