De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence.

Journal Article

The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly alpha-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.

Full Text

Duke Authors

Cited Authors

  • Hecht, MH; Richardson, JS; Richardson, DC; Ogden, RC

Published Date

  • August 24, 1990

Published In

Volume / Issue

  • 249 / 4971

Start / End Page

  • 884 - 891

PubMed ID

  • 2392678

Pubmed Central ID

  • 2392678

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.2392678


  • eng

Conference Location

  • United States