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
AUTHORS (7)
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.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (31)
CITATIONS (700)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....