title: A Single Stereodynamic Center Modulates the Rate of Self-Assembly in a Biomolecular System.
abstract: Chirality is a property of asymmetry important to both physical and abstract systems. Understanding how molecular systems respond to perturbations in their chiral building blocks can provide insight into diverse areas such as biomolecular self-assembly, protein folding, drug design, materials, and catalysis. Despite the fundamental importance of stereochemical preorganization in nature and designed materials, the ramifications of replacing chiral centers with stereodynamic atomic mimics in the context of biomolecular systems is unknown. Herein, we demonstrate that replacement of a single amino acid stereocenter with a stereodynamic nitrogen atom has profound consequences on the self-assembly of a biomolecular system. Our results provide insight into how the fundamental biopolymers of life would behave if their chiral centers were not configurationally stable, highlighting the vital importance of stereochemistry as a pre-organizing element in biomolecular folding and assembly events.
authors.affiliation: Department of Chemistry, University of Pennsylvania, 231 South 34thStreet, Philadelphia, PA 19104 (USA).
authors.forename: Yitao
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Department of Chemistry, University of Pennsylvania, 231 South 34thStreet, Philadelphia, PA 19104 (USA).
authors.forename: Roy M
authors.initials: RM
authors.lastname: Malamakal
authors.affiliation: Department of Chemistry, University of Pennsylvania, 231 South 34thStreet, Philadelphia, PA 19104 (USA). dcheno@sas.upenn.edu.
authors.forename: David M
authors.initials: DM
authors.lastname: Chenoweth
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D001704:Biopolymers / Q000737:chemistry*; D017510:Protein Folding; D013237:Stereoisomerism
chemical_list: D000596:Amino Acids; D001704:Biopolymers
keywords: chirality; collagen; protein folding; self-assembly; triple helix