Knowles, TP and Fitzpatrick, AW and Meehan, S and Mott, HR and Vendruscolo, M and Dobson, CM and Welland, ME (2007) Role of intermolecular forces in defining material properties of protein nanofibrils. Science, 318. pp. 1900-1903.Full text not available from this repository.
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.
|Uncontrolled Keywords:||Amyloid Amyloid beta-Peptides Chemistry, Physical Elasticity Humans Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Insulin Lactalbumin Lactoglobulins Microscopy, Atomic Force Models, Molecular Muramidase Nanostructures Peptide Termination Factors Peptides Physicochemical Phenomena Prealbumin Prions Protein Conformation Protein Structure, Tertiary Saccharomyces cerevisiae Proteins Surface Tension alpha-Crystallin B Chain|
|Divisions:||Div B > Solid State Electronics and Nanoscale Science|
|Depositing User:||Cron Job|
|Date Deposited:||15 Dec 2015 12:51|
|Last Modified:||01 May 2016 02:31|