Surface Ordering of Proteins Adsorbed on Graphite

The surface-induced rearrangement of distant protein strands adsorbed on a hydrophobic graphite surface is investigated through atomistic molecular dynamics simulations and energy minimizations. We show that fragments both of globular proteins consisting of either α-helices or β-sheets and of a fibr...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2004-09, Vol.108 (36), p.13850-13854
Main Authors: Raffaini, Giuseppina, Ganazzoli, Fabio
Format: Article
Language:English
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Summary:The surface-induced rearrangement of distant protein strands adsorbed on a hydrophobic graphite surface is investigated through atomistic molecular dynamics simulations and energy minimizations. We show that fragments both of globular proteins consisting of either α-helices or β-sheets and of a fibrous protein containing a triple helix do form parallel strands on this surface, irrespective of their native structure. On the other hand, a new secondary structure consisting of β-sheets lying on the surface was never observed even after a long simulation time. The parallel ordering is characteristic of graphite being absent, for instance, on a hydrophilic poly(vinyl alcohol) surface. Our simulations indicate that this result is not related to the surface rigidity, and we suggest that it is due to a combination of the surface hydrophobicity, crystallinity, and smoothness.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp0477452