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Self‐Assembly and Dynamics of Polypeptides
Author(s) -
Floudas George,
Spiess Hans Wolfgang
Publication year - 2009
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.200800700
Subject(s) - hydrogen bond , persistence (discontinuity) , protein secondary structure , persistence length , molecular dynamics , chemical physics , glass transition , peptide , self assembly , dynamic light scattering , dielectric , materials science , crystallography , dynamics (music) , scattering , chemistry , nanotechnology , molecule , physics , computational chemistry , composite material , polymer , optics , optoelectronics , organic chemistry , biochemistry , geotechnical engineering , nanoparticle , acoustics , engineering
This work highlights the results of recent efforts to understand the hierarchical self‐assembly and dynamics of polypeptides with the aid of different NMR techniques, X‐ray scattering, and dielectric spectroscopy. The concerted application of these techniques sheds light on the origin of the glass transition, the persistence of the α ‐helical peptide secondary motif, and the effects of topology and packing on the type and persistence of secondary structures. With respect to the freezing of the dynamics at the liquid‐to‐glass temperature it was found that the origin of this effect is a network of defected hydrogen bonds. The presence of defected hydrogen‐bonded regions reduces the persistence length of α ‐helices. Block copolypeptides provide means to manipulate both the type and persistence of peptide secondary structures.