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

Overview

abstract

  • Significance; The ability to construct novel proteins from basic principles of molecular structure is the fundamental goal of protein design. This is particularly challenging in the case of the β-barrel outer membrane proteins, where our understanding of the rules governing structure and function lags behind that of other classes of proteins. Here, we took a step toward understanding β-barrel membrane protein architecture by focusing on the outward-facing amino acid positions that contact the cell membrane. We replaced the membrane-facing surface of OmpA with new surfaces designed to resemble natural β-barrel surfaces. We were able to design versions of OmpA with mutations at about two-thirds of all surface positions, indicating that β-barrel membrane protein surface design is achievable.

publication date

  • August 4, 2015

has restriction

  • hybrid

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

volume

  • 112

issue

  • 31