AbstractThe unique sequence of the α‐chain is the structural cornerstone of the collagen triple helix that dictates its conformation and molecular behavior. In this study, collagen‐like peptides of varying sequence characteristics were designed to elucidate the role of Ser (polar residues), Ala (non‐polar residues), and Arg/Glu (ionizable residues) in the formation, kinetics, and stability of the triple helix, and its self‐assembly behavior. We found that the introduction of other common amino acids in (Gly‐Hyp‐Pro)n results in varying d...
