Spatial persistence of angular correlations in amyloid fibrils.
Using atomic force microscopy height maps, we resolve and quantify torsional fluctuations in one-dimensional amyloid fibril aggregates self-assembled from three different representative polypeptide systems. Furthermore, we show that angular correlation in these nanoscale structures is maintained over several microns, corresponding to many thousands of molecules along the fibril axis. We model disorder in the fibril in respect of both thermal fluctuations and structural defects, and determine quantitative values for the defect density, as well as the energy scales involved in the fundamental interactions stabilizing these generic structures.
Knowles
Tuomas P J
TP
Cavendish Laboratory, University of Cambridge, Cambridge CB3 OHE, United Kingdom and Nanoscience Centre, University of Cambridge, Cambridge CB3 OFF, United Kingdom.
Smith
Jeffrey F
JF
Craig
Aidan
A
Dobson
Christopher M
CM
Welland
Mark E
ME
D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D018625:Microscopy, Atomic Force; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D011487:Protein Conformation; D013223:Statistics as Topic
D000682:Amyloid