@article{10369,
  abstract     = {Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell.},
  author       = {Simunovic, Mijo and Šarić, Anđela and Henderson, J. Michael and Lee, Ka Yee C. and Voth, Gregory A.},
  issn         = {2374-7951},
  journal      = {ACS Central Science},
  keywords     = {general chemical engineering, general chemistry},
  number       = {12},
  pages        = {1246--1253},
  publisher    = {American Chemical Society},
  title        = {{Long-range organization of membrane-curving proteins}},
  doi          = {10.1021/acscentsci.7b00392},
  volume       = {3},
  year         = {2017},
}