Computational redesign of the lipid-facing surface of the outer membrane protein OmpA
Protein design
Folding (DSP implementation)
Protein Engineering
Peripheral membrane protein
Cell membrane
DOI:
10.1073/pnas.1501836112
Publication Date:
2015-07-22T02:10:15Z
AUTHORS (3)
ABSTRACT
Significance The ability to construct novel proteins from basic principles of molecular structure is the fundamental goal protein design. This particularly challenging in case β-barrel outer membrane proteins, where our understanding rules governing and function lags behind that other classes proteins. Here, we took a step toward architecture by focusing on outward-facing amino acid positions contact cell membrane. We replaced membrane-facing surface OmpA with new surfaces designed resemble natural surfaces. were able design versions mutations at about two-thirds all positions, indicating achievable.
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