With recent advances in X-ray crystallography of membrane proteins promising many new high-resolution structures, MD simulations become increasingly valuable for understanding membrane protein function, as they can unleash dynamic behavior concealed in the static structures. Dramatic increase in computational power in synergy with more efficient computational methodologies allows one today to carry out molecular dynamics simulations of any structurally known membrane protein in its native environment, covering the time scale of up to 0.1 μsec. At the frontier of membrane protein simulations are ion channels, aquaporins, passive and active transporters, and bioenergetic proteins. In this review we summarize recent developments in this rapidly evolving field.