English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We calculate potentials of the mean force for 20 amino acids in the vicinity of the (111) surface of gold, for several dipeptides, and for some analogues of the side chains, using molecular dynamics simulations and the umbrella sampling method. We compare results obtained within three different force fields: one hydrophobic (for a contaminated surface) and two hydrophilic. All of these fields lead to good binding with very different specificities and different patterns in the density and polarization of water. The covalent bond with the sulfur atom on cysteine is modeled by the Morse potential. We demonstrate that binding energies of dipeptides are different than the combined binding energies of their amino acidic components. For the hydrophobic gold, adsorption events of a small protein are driven by attraction to the strongest binding amino acids. This is not so in the hydrophilic cases—a result of smaller specificities combined with the difficulty for proteins, but not for single amino acids, to penetr...

Aqueous Amino Acids and Proteins Near the Surface of Gold in Hydrophilic and Hydrophobic Force Fields