4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins.

ABSTRACT: Proline is unique among proteinogenic amino acids because a pyrrolidine ring links its amino group to its side chain. This heterocycle constrains the conformations of the main chain and thus templates particular secondary structures. Proline residues undergo post-translational modification at the 4-position to yield 4-hydroxyproline, which is especially prevalent in collagen. Interest in characterizing the effects of this modification led to the use of 4-fluoroprolines to enhance inductive properties relative to the hydroxyl group of 4-hydroxyproline and to eliminate contributions from hydrogen bonding. The strong inductive effect of the fluoro group has three main consequences: enforcing a particular pucker upon the pyrrolidine ring, biasing the conformation of the preceding peptide bond,

SUBMITTER: Newberry RW 

PROVIDER: S-EPMC5501414 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature