Computational redesign of the lipid-facing surface of the outer membrane protein OmpA Journal Article uri icon



  • Advances in computational design methods have made possible extensive engineering of soluble proteins, but designed β-barrel membrane proteins await improvements in our understanding of the sequence determinants of folding and stability. A subset of the amino acid residues of membrane proteins interact with the cell membrane, and the design rules that govern this lipid-facing surface are poorly understood. We applied a residue-level depth potential for β-barrel membrane proteins to the complete redesign of the lipid-facing surface ofEscherichia coliOmpA. Initial designs failed to fold correctly, but reversion of a small number of mutations indicated by backcross experiments yielded designs with substitutions to up to 60% of the surface that did support folding and membrane insertion.

publication date

  • August 4, 2015

Date in CU Experts

  • September 24, 2019 5:00 AM

Full Author List

  • Stapleton JA; Whitehead TA; Nanda V

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0027-8424

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Additional Document Info

start page

  • 9632

end page

  • 9637


  • 112


  • 31