The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
De Novo Protein Design: Fully Automated Sequence Selection
Abstract
The first fully automated design and experimental validation of a novel sequence for an entire protein is described. A computational design algorithm based on physical chemical potential functions and stereochemical constraints was used to screen a combinatorial library of 1.9 × 10 27 possible amino acid sequences for compatibility with the design target, a ββα protein motif based on the polypeptide backbone structure of a zinc finger domain. A BLAST search shows that the designed sequence, full sequence design 1 (FSD-1), has very low identity to any known protein sequence. The solution structure of FSD-1 was solved by nuclear magnetic resonance spectroscopy and indicates that FSD-1 forms a compact well-ordered structure, which is in excellent agreement with the design target structure. This result demonstrates that computational methods can perform the immense combinatorial search required for protein design, and it suggests that an unbiased and quantitative algorithm can be used in various structural contexts.
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
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
Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163
Machine-learning-guided directed evolution for protein engineering
Yang, K. K., Wu, Z., & Arnold, F. H. (2019) · Nature Methods · doi:10.1038/s41592-019-0496-6 · Cited by 1,130
Shapovalov, M. V., & Dunbrack, R. L. (2011) · Structure · doi:10.1016/j.str.2011.03.019 · Cited by 1,000
Designing a 20-residue protein
Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793
Metadata
- Authors
- Dahiyat, B. I., & Mayo, S. L.
- Venue
- Science
- Published
- 1997-10-03
- Volume
- 278
- Issue
- 5335
- Pages
- 82-87
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085497102
- Cited by
- 1,145
- References
- 2
- FWCI
- 14.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Dahiyat, B. I., & Mayo, S. L. (1997). De Novo Protein Design: Fully Automated Sequence Selection. Science. https://doi.org/10.1126/science.278.5335.82
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
