The DOI matches its Crossref record; 158 of the 158 references it cites were found in a registry or an index.
Coiled-Coil Design: Updated and Upgraded
Abstract
α-Helical coiled coils are ubiquitous protein-folding and protein-interaction domains in which two or more α-helical chains come together to form bundles. Through a combination of bioinformatics analysis of many thousands of natural coiled-coil sequences and structures, plus empirical protein engineering and design studies, there is now a deep understanding of the sequence-to-structure relationships for this class of protein architecture. This has led to considerable success in rational design and what might be termed in biro de novo design of simple coiled coils, which include homo- and hetero-meric parallel dimers, trimers and tetramers. In turn, these provide a toolkit for directing the assembly of both natural proteins and more complex designs in protein engineering, materials science and synthetic biology. Moving on, the increased and improved use of computational design is allowing access to coiled-coil structures that are rare or even not observed in nature, for example α-helical barrels, which comprise five or more α-helices and have central channels into which different functions may be ported. This chapter reviews all of these advances, outlining improvements in our knowledge of the fundamentals of coiled-coil folding and assembly, and highlighting new coiled coil-based materials and applications that this new understanding is opening up. Despite considerable progress, however, challenges remain in coiled-coil design, and the next decade promises to be as productive and exciting as the last.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Since there is a small spacing deviation between 3.5 in heptad repeats and 3.6 in ideal α-helices, the hydrophobic face of a helix with 3.5 spacing proceeds around the helix, leading to supercoiling of helices upon assembly rather than packing in a straight manner.6”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [6]
Citations
Cites
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
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
X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil
O’Shea, E. K., Klemm, J. D., Kim, P. S., & Alber, T. (1991) · Science · doi:10.1126/science.1948029 · Cited by 1,444
Coiled coils: new structures and new functions
Lupas, A. N. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10052-9 · Cited by 1,321
Koronakis, V. E., Sharff, A., Koronakis, E., Luisi, B. F., & Hughes, C. (2000) · Nature · doi:10.1038/35016007 · Cited by 1,086
The α-helix dipole and the properties of proteins
Hol, W. G. J., van Duijnen, P. T., & Berendsen, H. J. C. (1978) · Nature · doi:10.1038/273443a0 · Cited by 1,007
The Structure of α-Helical Coiled Coils
Lupas, A. N., & Gruber, M. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(05)70003-6 · Cited by 681
Computational Design of Self-Assembling Protein Nanomaterials with Atomic Level Accuracy
King, N. P., Sheffler, W., Sawaya, M. R., Vollmar, B. S., Sumida, J. P., André, I., Gonen, T., Yeates, T. O., & Baker, D. A. (2012) · Science · doi:10.1126/science.1219364 · Cited by 655
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
Self-citation
Cited by
Sorted by citations
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 348
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A. O., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 334
Recent advances in de novo protein design: Principles, methods, and applications
Pan, X., & Kortemme, T. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100558 · Cited by 228
Power to the protein: enhancing and combining activities using the Spy toolbox
Keeble, A. H., & Howarth, M. R. (2020) · Chemical Science · doi:10.1039/d0sc01878c · Cited by 189
DeepCoil—a fast and accurate prediction of coiled-coil domains in protein sequences
Ludwiczak, J., Winski, A., Szczepaniak, K., Alva, V., & Dunin-Horkawicz, S. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty1062 · Cited by 189
Metadata
- Authors
- Woolfson, D. N.
- Affiliations
- University of Bristol (GB)
- Corresponding author
- Woolfson, Derek N.
- ORCID
- Woolfson, Derek N.
- Venue
- Subcellular Biochemistry
- Publisher
- Springer International Publishing
- Published
- 2017
- Volume
- 82
- Pages
- 35-61
- ISSN
- 0306-0225 (ISSN-L)
- OpenAlex
- W2579233876
- Cited by
- 149
- References
- 158
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 14 · 2023: 24 · 2022: 18 · 2021: 27 · 2020: 18 · 2019: 9 · 2018: 16 · 2017: 9
- FWCI
- 17.68
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Explore Bristol Research (submittedVersion)
- Bristol Research (University of Bristol) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/L01386X/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- alpha-helical coiled coil, protein folding, protein-protein interaction domains, rational protein design, de novo protein design, protein assembly, synthetic biology, protein-based materials
- MeSH terms
- Protein Conformation, alpha-Helical, Animals, Humans, Models, Molecular, Proteins, Protein Folding, Protein Interaction Domains and Motifs
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
