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Computational design of water-soluble α-helical barrels
Open accessAbstract
The design of protein sequences that fold into prescribed de novo structures is challenging. General solutions to this problem require geometric descriptions of protein folds and methods to fit sequences to these. The α-helical coiled coils present a promising class of protein for this and offer considerable scope for exploring hitherto unseen structures. For α-helical barrels, which have more than four helices and accessible central channels, many of the possible structures remain unobserved. Here, we combine geometrical considerations, knowledge-based scoring, and atomistic modeling to facilitate the design of new channel-containing α-helical barrels. X-ray crystal structures of the resulting designs match predicted in silico models. Furthermore, the observed channels are chemically defined and have diameters related to oligomer state, which present routes to design protein function.
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“However, the majority of de novo designed coiled coils are hyperstable, with melting points exceeding 100 °C.11,12”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [12]
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Self-citation
Metadata
- Authors
- Thomson, A. R., Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L., & Woolfson, D. N.
- Affiliations
- University of Bristol (GB)
- Corresponding author
- Thomson, Andrew R.
- Wood, Christopher W.
- Burton, Antony J.
- Woolfson, Derek N.
- ORCID
- Venue
- Science
- Published
- 2014-10-24
- Volume
- 346
- Issue
- 6208
- Pages
- 485-488
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1834588461
- Cited by
- 330
- References
- 40
- Citations by year
- 2026: 11 · 2025: 19 · 2024: 21 · 2023: 17 · 2022: 30 · 2021: 35 · 2020: 35 · 2019: 36 · 2018: 27 · 2017: 41 · 2016: 41 · 2015: 14 · 2014: 3
- FWCI
- 13.54
- Type
- journal article
- Language
- en
- Open access
- Licence
- other-oa
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Bristol Research (University of Bristol) (submittedVersion, other-oa)
- Funders
- Engineering and Physical Sciences Research Council (EP/K03927X/1, EP/J001430/1, 1115150)
- Biotechnology and Biological Sciences Research Council (BB/L01386X/1, BB/J008990/1, 1228976)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- de novo protein design, coiled coil, protein folding, knowledge-based scoring, water-soluble proteins, protein oligomerization, atomistic modeling
- MeSH terms
- Models, Molecular, Peptides, Solubility, Water, Protein Structure, Secondary, Computational Biology
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