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• W1967742306 abstract "The self-assembly mechanism and the associated molecular dynamics are studied for a series of poly-l-lysine-functionalized polyphenylene dendrimer melts as a function of the core size (generation), functionality, and polypeptide length using X-rays, solid-state NMR, calorimetry, and dielectric spectroscopy. A striking dependence of the polyphenylene self-assembly on the poly-l-lysine length is shown. In addition, the type (α-helix/β-sheet) of peptide secondary structure is controlled by the packing restrictions imposed by the polyphenylene core. We show that constrained poly-l-lysines can adopt different secondary structures from their linear analogues. The dynamic investigation revealed significant mobility associated solely with the polypeptide through three processes: a glass transition, a slower process associated with the relaxation of α-helical segments, and a glassy mode whose origin could be resolved by site-specific solid-state NMR techniques. Solid-state NMR studies further indicated a mobility gradient in going from the rigid peptide backbone to the side chains." @default.
• W1967742306 created "2016-06-24" @default.
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• W1967742306 date "2006-12-01" @default.
• W1967742306 modified "2023-09-29" @default.
• W1967742306 title "Self-Assembly and Molecular Dynamics of Peptide-Functionalized Polyphenylene Dendrimers" @default.
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• W1967742306 doi "https://doi.org/10.1021/ma0621270" @default.
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