Proteomimetic Zinc Finger Domains with Modified Metal-binding β-Turns.

ABSTRACT: The mimicry of protein tertiary folds by chains artificial in backbone chemical composition leads to proteomimetic analogues with potential utility as bioactive agents and as tools to shed light on biomacromolecule behavior. Notable successes toward such molecules have been achieved; however, as protein structural diversity is vast, design principles must be continually honed as they are applied to new prototype folding patterns. One specific structure where a gap remains in understanding how to effectively generate modified backbone analogues is the metal-binding β-turn found in zinc finger domains. Literature precedent suggests several factors that may act in concert, including the artificial moiety used to modify the turn, the sequence in which it is applied, and modifications present e

SUBMITTER: Rao SR 

PROVIDER: S-EPMC7958900 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature