Visiting order on membrane proteins by using nanotechnology

摘要: During the past decade, there has been spectacular progress in membrane protein structural biology, with number of determined structures increasing by an order magnitude to more than 100 (1). Most multispan integral proteins (IMPs) have using x-ray crystallography. However, solution NMR methods also provided a modest for both α-helical and β-barrel IMPs, ranging up 30 kDa molecular mass (2, 3). Moreover, momentum solid-state (4, 5) IMPs is growing, thanks part iterative innovation between pulse technology sample preparation/manipulation. In latter category important new method achieve marginal alignment proteins, as introduced this issue PNAS Douglas et al. (6). Marginal prerequisite experimentally accessing rich source restraints: residual dipolar couplings (RDC). This novel can be predicted significantly extend which RDC accessed well enhance ease accuracy are measured.