Answers are grounded in this paper and cite their sources.
The 'protein world' exhibits additional complexity caused by post-translational modifications. One such process is nonenzymic deamidation of asparagine which is controlled partly by primary sequence, but also higher order protein structure. We have studied the deamidation of an N-terminal peptide in muscle glyceraldehyde 3-phosphate dehydrogenase to relate three-dimensional structure, proteolysis, and deamidation. This work has significant consequences for identification of proteins using peptide mass fingerprinting.
No takes yet. Share an insight, caveat, or question.
Rivers et al. (2008) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: