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Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

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Science  21 Dec 2007:
Vol. 318, Issue 5858, pp. 1900-1903
DOI: 10.1126/science.1150057

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Abstract

Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.

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