Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.

ABSTRACT: β-Amino acids have a backbone that is expanded by one carbon atom relative to α-amino acids, and β residues have been investigated as subunits in protein-like molecules that adopt discrete and predictable conformations. Two classes of β residue have been widely explored in the context of generating α-helix-like conformations: β³ -amino acids, which are homologous to α-amino acids and bear a side chain on the backbone carbon adjacent to nitrogen, and residues constrained by a five-membered ring, such the one derived from trans-2-aminocyclopentanecarboxylic acid (ACPC). Substitution of α residues with their β³  homologues within an α-helix-forming sequence generally causes a decrease in conformational stability. Use of a ring-constrained β residue, however, can offset t

SUBMITTER: Mortenson DE 

PROVIDER: S-EPMC5944345 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature