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Computational design of water-soluble α-helical barrels

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Thomson, Andrew R., Wood, Christopher W., Burton, Antony J., Bartlett, Gail J., Sessions, Richard B., Brady, R. Leo, Woolfson, Derek N.·2014·Science

DOI 10.1126/science.1257452

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Abstract

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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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: Thomson, Andrew R.
Wood, Christopher W.
Burton, Antony J.
Bartlett, Gail J.
Sessions, Richard B.
Brady, R. Leo
Woolfson, Derek N.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2014-10-24
Volume: 346
Issue: 6208
Pages: 485-488
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1257452
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: green
research-information.bris.ac.uk
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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Computational design of water-soluble α-helical barrels

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