TY - JOUR
TI - Conformational transitions of poly(l-proline) in copolypeptides with poly(γ-benzyl-l-glutamate) induced by packing
AU - R. Graf
AU - H. W. Spiess
AU - G. Floudas
AU - H.-J. Butt
AU - M. Gkikas
AU - H. Iatrou
JO - Macromolecules
PY - 2012
VL - 45
TODO - 23
SP - 9326--9332
PB - American Chemical Society (ACS)
SN - 0024-9297, 1520-5835
TODO - 10.1021/ma301906m
TODO - 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
TODO - 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.
ER -