Jump to main content
Jump to site search

Issue 36, 2017
Previous Article Next Article

Proteins at air–water and oil–water interfaces in an all-atom model

Author affiliations

Abstract

We study the behavior of five proteins at the air–water and oil–water interfaces by all-atom molecular dynamics. The proteins are found to get distorted when pinned to the interface. This behavior is consistent with the phenomenological way of introducing the interfaces in a coarse-grained model through a force that depends on the hydropathy indices of the residues. Proteins couple to the oil–water interface stronger than to the air–water one. They diffuse slower at the oil–water interface but do not depin from it, whereas depinning events are observed at the other interface. The reduction of the disulfide bonds slows the diffusion down.

Graphical abstract: Proteins at air–water and oil–water interfaces in an all-atom model

Back to tab navigation

Supplementary files

Publication details

The article was received on 07 Jun 2017, accepted on 03 Sep 2017 and first published on 04 Sep 2017


Article type: Paper
DOI: 10.1039/C7CP03829A
Citation: Phys. Chem. Chem. Phys., 2017,19, 25197-25206
  •   Request permissions

    Proteins at air–water and oil–water interfaces in an all-atom model

    Y. Zhao and M. Cieplak, Phys. Chem. Chem. Phys., 2017, 19, 25197
    DOI: 10.1039/C7CP03829A

Search articles by author

Spotlight

Advertisements