We study two distinctly ordered condensed phases of polypeptide molecules, amyloid fibrils and amyloidlike microcrystals, and the first-order twisting phase transition between these two states. We derive a single free-energy form which connects both phases. Our model identifies relevant degrees of freedom for describing the collective behavior of supramolecular polypeptide structures, reproduces accurately the results from molecular dynamics simulations as well as from experiments, and sheds light on the uniform nature of the dimensions of different peptide fibrils. © 2012 American Physical Society.
Twisting transition between crystalline and fibrillar phases of aggregated peptides / Knowles, T. P. J.; De Simone, A.; Fitzpatrick, A. W.; Baldwin, A.; Meehan, S.; Rajah, L.; Vendruscolo, M.; Welland, M. E.; Dobson, C. M.; Terentjev, E. M.. - In: PHYSICAL REVIEW LETTERS. - ISSN 0031-9007. - 109:15(2012). [10.1103/PhysRevLett.109.158101]
Twisting transition between crystalline and fibrillar phases of aggregated peptides
De Simone A.;
2012
Abstract
We study two distinctly ordered condensed phases of polypeptide molecules, amyloid fibrils and amyloidlike microcrystals, and the first-order twisting phase transition between these two states. We derive a single free-energy form which connects both phases. Our model identifies relevant degrees of freedom for describing the collective behavior of supramolecular polypeptide structures, reproduces accurately the results from molecular dynamics simulations as well as from experiments, and sheds light on the uniform nature of the dimensions of different peptide fibrils. © 2012 American Physical Society.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
