Atomic-level description of protein-lipid interactions using an accelerated membrane model.

摘要: Peripheral membrane proteins are structurally diverse that involved in fundamental cellular processes. Their activity of these is frequently modulated through their interaction with membranes, and as a result techniques to study the interfacial between peripheral high demand. Due fluid nature reversibility protein-membrane interactions, experimental systems remains challenging task. Molecular dynamics simulations offer suitable approach protein-lipid interactions; however, slow lipids often prevents sufficient sampling specific membrane-protein interactions atomistic simulations. To increase lipid while preserving detail highly mobile membrane-mimetic (HMMM) model core replaced by an organic solvent, short-tailed provide nearly complete representation natural at solvent/water interface. Here, we present brief introduction summary recent applications HMMM different proteins, complementing characterization presented systems, perspective future other classes proteins. This article part Special Issue entitled: Membrane edited J.C. Gumbart Sergei Noskov.