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Cited by 390

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

De Novo Design, Expression, and Characterization of Felix: a Four-Helix Bundle Protein of Native-Like Sequence

Hecht, Michael H., Richardson, Jane S., Richardson, David C., Ogden, Richard C.·1990·Science

Abstract

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 α-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.

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Crossref · 10.1126/science.2392678

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Metadata

Authors
Hecht, M. H., Richardson, J. S., Richardson, D. C., & Ogden, R. C.
Venue
Science
Published
1990-08-24
Volume
249
Issue
4971
Pages
884-891
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2089958448
Cited by
390
References
1
FWCI
7.56
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: De Novo Design, Expression, and Characterization of Felix: a Four-Helix Bundle Protein of Native-Like Sequence. https://app.cochat.ai/papers/10.1126/science.2392678
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Hecht, M. H., Richardson, J. S., Richardson, D. C., & Ogden, R. C. (1990). De Novo Design, Expression, and Characterization of Felix: a Four-Helix Bundle Protein of Native-Like Sequence. Science. https://doi.org/10.1126/science.2392678

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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