@article{2959206,
    title = "Conformational transitions of poly(l-proline) in copolypeptides with poly(γ-benzyl-l-glutamate) induced by packing",
    author = "R. Graf and H. W. Spiess and G. Floudas and H.-J. Butt and M. Gkikas and H. Iatrou",
    journal = "Macromolecules",
    year = "2012",
    volume = "45",
    number = "23",
    pages = "9326--9332",
    publisher = "American Chemical Society (ACS)",
    issn = "0024-9297, 1520-5835",
    doi = "10.1021/ma301906m",
    keywords = "Bulk properties;  Conformational change;  Conformational transitions;  Copolypeptides;  Hexagonal cells;  Hierarchical self-assembly;  L-proline;  Proline residues;  Solid state NMR;  Steric hindrances, Hydrogen bonds;  Polypeptides, Amino acids",
    abstract = "The hierarchical self-assembly and dynamics of poly(γ-benzyl-l- glutamate)-b-poly(l-proline) (PBLG-b-PLP) polypeptides are investigated with X-rays and solid state NMR. Both blocks possess helices stabilized solely either by hydrogen bonds (PBLG) or by steric hindrance (PLP) and are further packed in two different hexagonal cells. We report a trans/cis conformational change of PLP upon confinement that mimics the isomerization of isolated proline residues in proteins. These cis PLP conformations reside primarily at the PLP/PBLG interface, alleviate the packing frustration, and permit PBLG and PLP helices to pack with their bulk properties. © 2012 American Chemical Society."
}