Aza-proline effectively mimics l-proline stereochemistry in triple helical collagen.

ABSTRACT: The prevalence of l-amino acids in biomolecules has been shown to have teleological importance in biomolecular structure and self-assembly. Recently, biophysical studies have demonstrated that natural l-amino acids can be replaced with non-natural achiral aza-amino acids in folded protein structures such as triple helical collagen. However, the structural consequences of achiral aza-amino acid incorporation has not been elucidated in the context of any relevant folded biomolecule. Herein, we use X-ray crystallography to provide the first atomic resolution crystal structure of an achiral aza-amino acid residue embedded within a folded protein structure, definitively illustrating that achiral aza-proline has the capacity to effectively mimic the stereochemistry of natural amino acids within

SUBMITTER: Kasznel AJ 

PROVIDER: S-EPMC6761869 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature