1flx

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

DE NOVO DESIGN, EXPRESSION, AND CHARACTERIZATION OF FELIX: A FOUR-HELIX BUNDLE PROTEIN OF NATIVE-LIKE SEQUENCE

spinqualitylabelsall models 1flx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed 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. De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence.,Hecht MH, Richardson JS, Richardson DC, Ogden RC Science. 1990 Aug 24;249(4971):884-91. PMID:2392678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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