The Regulation of Biological Processes Two of the 20 ordinarily occurring amino acid residues in peptides and proteins are inherently unstable in physiological solutions. These glutaminyl and asparaginyl residues undergo deamidation to become glutamic acid and aspartic acid residues under laboratory conditions and also in the cells of plants and animals. It was originally proposed by Dr. Robinson that deamidations of these residues may serve as molecular clocks by which the processes of protein turnover, development, and aging are timed in living things.
 It has since been shown that deamidation of glutaminyl and asparaginyl residues can control widely different timed intervals by means of different genetic variations in protein sequence and three-dimensional structure. It has also been discovered that deamidation controls the turnover rates of some proteins in living things. Institute scientists have published a substantial amount of original research on this subject and are continuing to work toward a further understanding of deamidation and its potential role as a fundamentally important molecular clock for the regulation of biological processes.
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Oregon Institute of Science and Medicine |
