title: Secondary structure and protein deamidation.
abstract: The deamidation reactions of asparagine residues in alpha-helical and beta-turn secondary structural environments of peptides and proteins are reviewed. Both kinds of secondary structure tend to stabilize asparagine residues against deamidation, although the effects are not large. The effect of beta-sheet structures on asparagine stability is unclear, although simple considerations suggest a stabilization in this environment also.
authors.affiliation: Department of Pharmaceutical Chemistry, Simons Laboratories of the Higuchi Biosciences Center, University of Kansas, Lawrence, Kansas, 66047, USA.
authors.forename: M
authors.initials: M
authors.lastname: Xie
authors.forename: R L
authors.initials: RL
authors.lastname: Schowen
mesh_terms: D000577:Amides / Q000378:metabolism*; D000818:Animals; D001216:Asparagine / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000577:Amides; D011506:Proteins; D001216:Asparagine