The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
High-Resolution Protein Design with Backbone Freedom
Abstract
Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of α-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form α-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.
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Citations
Cites
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Self-citationThe Fourier transform of a coiled-coil
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001952 · Cited by 313
Cited by
The coming of age of de novo protein design
Huang, P.-S., Boyken, S. E., & Baker, D. (2016) · Nature · doi:10.1038/nature19946 · Cited by 1,478
Advances in protein structure prediction and design
Kuhlman, B., & Bradley, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0163-x · Cited by 806
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Principles for designing ideal protein structures
Koga, N., Tatsumi-Koga, R., Liu, G., Xiao, R., Acton, T. B., Montelione, G. T., & Baker, D. (2012) · Nature · doi:10.1038/nature11600 · Cited by 564
Protein Design by Directed Evolution
Jäckel, C., Kast, P., & Hilvert, D. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125832 · Cited by 409
Metadata
- Authors
- Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T., & Kim, P. S.
- Venue
- Science
- Published
- 1998-11-20
- Volume
- 282
- Issue
- 5393
- Pages
- 1462-1467
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2043883458
- Cited by
- 458
- References
- 3
- FWCI
- 7.77
- Type
- journal article
- Language
- en
- Open access
- closed
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- Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T., & Kim, P. S. (1998). High-Resolution Protein Design with Backbone Freedom. Science. https://doi.org/10.1126/science.282.5393.1462
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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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