Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

Rigidity (electromagnetism) Structural rigidity Side chain
DOI: 10.1126/science.1150057 Publication Date: 2007-12-21T01:19:52Z
ABSTRACT
Protein molecules have the ability to form a rich variety of natural and artificial structures materials. We show that amyloid fibrils, ordered supramolecular nanostructures are self-assembled from wide range polypeptide molecules, rigidities varying over four orders magnitude, constitute class high-performance biomaterials. elucidate molecular origin fibril material properties major contribution their rigidity stems generic interbackbone hydrogen-bonding network is modulated by variable side-chain interactions.
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