Labeling and Protecting N-Terminal Protein Positions by -Peptidyl Aminopeptidase-Catalyzed Attachment of -Amino-Acid Residues - Insulin as a First Example
HELVETICA CHIMICA ACTA(2018)
摘要
We have shown for the first time that a natural protein (human insulin) can be acylated at the N-terminus with a -amino acid (H-(3)hAla-), in a process catalyzed by the -peptidyl aminopeptidase 3-2W4-BapA. This selective modification, which could also be applied for protein labeling and tagging, should be generally useful, also to protect peptides and proteins from attack by common aminopeptidases.
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关键词
post-translational protein modification,reversible enzymatic N-terminal H-((3)hAla) attachment to a protein,-peptidyl aminopeptidase 3-2W4-BapA,insulin,peptide synthesis,solid-phase peptide synthesis (SPPS),coupling reagent DMT,NMM,TsO-
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