Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

By Tuomas P. J. Knowles, A. Fitzpatrick, Sarah Meehan, H. Mott, Michele Vendruscolo, Christopher M. Dobson, M. Welland. Science, 2007

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Nanomechanics of functional and pathological amyloid materials. (2011, background): “However, the presence of a surface or of interactions between individual structures has the potential to lead to fluctuations other than those given by simple thermal motion of individual fibrils, and can represent an experimental challeng”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “This generic nature (in which “generic” indicates common but not identical characteristics) can be attributed to the dominance of the main chain interactions common to all polypeptide molecules, with variations on this common theme resulting from differences in amino acid sequences and chain lengths”