The DOI matches its Crossref record.
The Fourier transform of a coiled-coil
Open accessAbstract
The Fourier transforms are given for a continuous coiled-coil, and for a set of atoms spaced a~ regular intervals along a coiled-coil.The nature of the solution is briefly discussed.
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
“Coiled coils can adopt a variety of parallel, antiparallel or mixed (e.g., up–down–up) topologies, which can be characterized with three geometric descriptors: the coiled coil radius, interface (Crick) angle and pitch (Figure 1A).2”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [2]
Citations
Cites
Still being checked.
Cited by
Sorted by citations
Intermediate filaments as mechanical integrators of cellular space
Lazarides, E. (1980) · Nature · doi:10.1038/283249a0 · Cited by 1,953
Atomic structure of the ectodomain from HIV-1 gp41
Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., & Wiley, D. C. (1997) · Nature · doi:10.1038/387426a0 · Cited by 1,625
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
Stability of proteins. Proteins which do not present a single cooperative system.
Privalov, P. L. (1982) · PubMed · Cited by 1,035
Macromolecular modeling and design in Rosetta: recent methods and frameworks
Leman, J. K., Weitzner, B. D., Lewis, S. M., Adolf-Bryfogle, J., Alam, N., Alford, R. F., Aprahamian, M., Baker, D., Barlow, K. A., Barth, P., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-0848-2 · Cited by 888
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
Privalov, P. L. (1982) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60468-4 · Cited by 745
Molecular Structure of Collagen
Ramachandran, G. N. (1963) · International review of connective tissue research · doi:10.1016/b978-1-4831-6755-8.50009-7 · Cited by 719
DNA bending and its relation to nucleosome positioning
Drew, H. R., & TRAVERS, A. A. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90396-1 · Cited by 706
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
Molecular conformation of poly(S‐lactic acid)
Santis, P. D., & Kovacs, A. J. (1968) · Biopolymers · doi:10.1002/bip.1968.360060305 · Cited by 575
De Novo Design and Structural Characterization of Proteins and Metalloproteins
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., & Lombardi, A. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.779 · Cited by 572
Atomic structure of a thermostable subdomain of HIV-1 gp41
Tan, K., Liu, J.-H., Wang, J., Shen, S. S., & Lu, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12303 · Cited by 534
Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472
The molecular biology of intermediate filaments
Steinert, P. M., Steven, A. C., & Roop, D. R. (1985) · Cell · doi:10.1016/0092-8674(85)90098-4 · Cited by 473
High-Resolution Protein Design with Backbone Freedom
Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T., & Kim, P. S. (1998) · Science · doi:10.1126/science.282.5393.1462 · Cited by 458
Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes
The May-Hegglin Fechtner Syndrome Consortium (2000) · Nature Genetics · doi:10.1038/79063 · Cited by 447
The Structure Of Collagen And Gelatin
Harrington, W. F., & von Hippel, P. H. (1962) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60028-5 · Cited by 400
Molecular Biology of Mineralized Tissues with Particular Reference to Bone
Glimcher, M. J. (1959) · Reviews of Modern Physics · doi:10.1103/revmodphys.31.359 · Cited by 393
Self-assembly of bovine epidermal keratin filaments in vitro
Steinert, P. M., Idler, W. W., & Zimmerman, S. B. (1976) · Journal of Molecular Biology · doi:10.1016/s0022-2836(76)80136-2 · Cited by 380
Paramyosin and the filaments of molluscan “catch” muscles
Szent‐Györgyi, A. G., Cohen, C., & Kendrick‐Jones, J. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90462-1 · Cited by 356
Pinto, L. H., Dieckmann, G. R., Gandhi, C. S., Papworth, C., Braman, J. C., Shaughnessy, M. A., Lear, J. D., Lamb, R. A., & DeGrado, W. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11301 · Cited by 352
Coiled‐coils: The long and short of it
Truebestein, L., & Leonard, T. A. (2016) · BioEssays · doi:10.1002/bies.201600062 · Cited by 338
Structure and interactions of biological helices
Kornyshev, A. A., Lee, D. J., Leikin, S., & Wynveen, A. (2007) · Reviews of Modern Physics · doi:10.1103/revmodphys.79.943 · Cited by 321
Crystal structure of dimeric HIV-1 capsid protein
Momany, C., Kovari, L. C., Prongay, A., Keller, W., Gitti, R. K., Lee, B. M., Gorbalenya, A. E., Tong, L., McClure, J., Ehrlich, L. S., et al. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0996-763 · Cited by 313
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
Crewther, W. G., Fraser, R., Lennox, F. G., & Lindley, H. (1965) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60390-3 · Cited by 306
De novo design of a transmembrane Zn 2+ -transporting four-helix bundle
Joh, N. H., Wang, T., Bhate, M., Acharya, R., Wu, Y., Grabe, M., Hong, M., Grigoryan, G., & DeGrado, W. F. (2014) · Science · doi:10.1126/science.1261172 · Cited by 301
The Crystal Structure of a Five-Stranded Coiled Coil in COMP: A Prototype Ion Channel?
Malashkevich, V. N., Kammerer, R. A., Efimov, V. P., Schulthess, T., & Engel, J. (1996) · Science · doi:10.1126/science.274.5288.761 · Cited by 301
Structural specificity in coiled-coil interactions
Grigoryan, G., & Keating, A. E. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.04.008 · Cited by 290
Apostolovic, B., Danial, M., & Klok, H. (2010) · Chemical Society Reviews · doi:10.1039/b914339b · Cited by 287
Applications of linear Dichroism Spectroscopy
Nordén, B. (1978) · Applied Spectroscopy Reviews · doi:10.1080/05704927808060393 · Cited by 284
Tropomyosin: Crystal structure, polymorphism and molecular interactions
Caspar, D. L. D., Cohen, C., & Longley, W. (1969) · Journal of Molecular Biology · doi:10.1016/0022-2836(69)90128-4 · Cited by 280
High thermodynamic stability of parametrically designed helical bundles
Huang, P.-S., Oberdorfer, G., Xu, C., Pei, X. Y., Nannenga, B. L., Rogers, J. M., DiMaio, F., Gonen, T., Luisi, B., & Baker, D. (2014) · Science · doi:10.1126/science.1257481 · Cited by 277
De novo design of bioactive protein switches
Langan, R. A., Boyken, S. E., Ng, A. H., Samson, J. A., Dods, G., Westbrook, A. M., Nguyen, T. H., Lajoie, M. J., Chen, Z., Berger, S., et al. (2019) · Nature · doi:10.1038/s41586-019-1432-8 · Cited by 268
Parry, D. A. D., Fraser, R. D. B., & Squire, J. M. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.01.016 · Cited by 264
Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-Å resolution
Malashkevich, V. N., Schneider, B. J., McNally, M. L., Milhollen, M. A., Pang, J. X., & Kim, P. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2662 · Cited by 261
De novo protein design, a retrospective
Korendovych, I. V., & DeGrado, W. (2020) · Quarterly Reviews of Biophysics (print) · doi:10.1017/s0033583519000131 · Cited by 173
Strelkov, S. V., & Burkhard, P. (2002) · Journal of Structural Biology · doi:10.1006/jsbi.2002.4454 · Cited by 246
Movement and self-control in protein assemblies. Quasi-equivalence revisited
Caspar, D. L. D. (1980) · Biophysical Journal · doi:10.1016/s0006-3495(80)84929-0 · Cited by 245
The Polypeptide Chain Configuration of Collagen
COWAN, P. M., McGavin, S., & North, A. C. T. (1955) · Nature · doi:10.1038/1761062a0 · Cited by 240
Probing Designability via a Generalized Model of Helical Bundle Geometry
Grigoryan, G., & DeGrado, W. F. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.058 · Cited by 232
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
Predicting coiled-coil regions in proteins
Lupas, A. N. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80056-5 · Cited by 231
The Structure and Chemistry of Keratin Fibers
Bradbury, J. (1973) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60447-7 · Cited by 229
Tao, Y. J., Strelkov, S. V., Mesyanzhinov, V. V., & Rossmann, M. G. (1997) · Structure · doi:10.1016/s0969-2126(97)00233-5 · Cited by 226
Coiled Coils – A Model System for the 21st Century
Lupas, A. N., & Baßler, J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.10.007 · Cited by 202
The bending of DNA in nucleosomes and its wider implications
TRAVERS, A. A., & Klug, A. (1987) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1987.0080 · Cited by 186
Programmable design of orthogonal protein heterodimers
Chen, Z., Boyken, S. E., Jia, M., Büsch, F., Flores‐Solis, D., Bick, M. J., Lu, P., VanAernum, Z. L., Sahasrabuddhe, A., Langan, R. A., et al. (2018) · Nature · doi:10.1038/s41586-018-0802-y · Cited by 178
Paramyosin and the filaments of molluscan “catch” muscles
Cohen, C., Szent-Györgyi, A. G., & Kendrick‐Jones, J. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90461-x · Cited by 178
Functions of intermediate filaments
Klymkowsky, M. W., Bachant, J. B., & Domingo, A. (1989) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970140302 · Cited by 178
Design and engineering of artificial oxygen-activating metalloenzymes
Nastri, F., Chino, M., Maglio, O., Bhagi‐Damodaran, A., Lu, Y., & Lombardi, A. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00923e · Cited by 177
Computational design of transmembrane pores
Xu, C., Lu, P., El-Din, T. M. G., Pei, X. Y., Johnson, M. C., Uyeda, A., Bick, M. J., Xu, Q. K., Jiang, D., Bai, H., et al. (2020) · Nature · doi:10.1038/s41586-020-2646-5 · Cited by 161
De novo design of fibrils made of short α-helical coiled coil peptides
Potekhin, S. A., Melnik, T. N., Popov, V. I., Lanina, N. F., Vazina, A. A., Rigler, P., Verdini, A. S., Corradin, G., & Kajava, A. V. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00073-4 · Cited by 163
Comparative analysis of coiled-coil prediction methods
Gruber, M., Söding, J., & Lupas, A. N. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.03.009 · Cited by 161
De novo design of tunable, pH-driven conformational changes
Boyken, S. E., Benhaim, M. A., Büsch, F., Jia, M., Bick, M. J., Choi, H., Klima, J. C., Chen, Z., Walkey, C., Mileant, A., et al. (2019) · Science · doi:10.1126/science.aav7897 · Cited by 163
Coiled-Coil Design: Updated and Upgraded
Woolfson, D. N. (2017) · Subcellular Biochemistry · doi:10.1007/978-3-319-49674-0_2 · Cited by 149
Characterization and sequence of the Escherichia coli stress-induced psp operon
Brissette, J. L., Weiner, L., Ripmaster, T. L., & Model, P. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90379-k · Cited by 147
X-ray diffraction studies of the molecular structure of nucleohistone and chromosomes
Wilkins, M. H. F., Zubay, G., & Wilson, H. R. (1959) · Journal of Molecular Biology · doi:10.1016/s0022-2836(59)80046-2 · Cited by 146
An Electron Microscope Study of Thin Sections of Human Skin
Selby, C. C. (1957) · Journal of Investigative Dermatology · doi:10.1038/jid.1957.80 · Cited by 144
Crystal structure and molecular interactions of tropomyosin
Phillips, G. N., Lattman, E. E., Cummins, P. L., Lee, K. Y., & Cohen, C. (1979) · Nature · doi:10.1038/278413a0 · Cited by 143
A super-coil model for nucleohistone
Paedon, J. F., & Wilkins, M. H. F. (1972) · Journal of Molecular Biology · doi:10.1016/0022-2836(72)90267-7 · Cited by 143
Historical review: Another 50th anniversary – new periodicities in coiled coils
Gruber, M. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.008 · Cited by 141
Chalkley, M. J., Mann, S. I., & DeGrado, W. F. (2021) · Nature Reviews Chemistry · doi:10.1038/s41570-021-00339-5 · Cited by 147
Structure of chitin-protein complexes: Ovipositor of the ichneumon fly Megarhyssa
Blackwell, J., & Weih, M. A. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90156-4 · Cited by 137
A phage repressor–operator complex at 7 Å resolution
Anderson, J. E., Ptashne, M., & Harrison, S. C. (1985) · Nature · doi:10.1038/316596a0 · Cited by 137
Harnessing self-assembled peptide nanoparticles in epitope vaccine design
Negahdaripour, M., Golkar, N., Hajighahramani, N., Kianpour, S., Nezafat, N., & Ghasemi, Y. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.05.002 · Cited by 134
Structure of the backbone in myosin filaments of muscle
Wray, J. S. (1979) · Nature · doi:10.1038/277037a0 · Cited by 131
C CB uilder 2.0: Powerful and accessible coiled‐coil modeling
Wood, C. W., & Woolfson, D. N. (2017) · Protein Science · doi:10.1002/pro.3279 · Cited by 131
COMPUTER-BASED DESIGN OF NOVEL PROTEIN STRUCTURES
Butterfoss, G. L., & Kuhlman, B. A. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102046 · Cited by 128
Structure and assembly of filamentous bacterial viruses
Marvin, D. A., & Wachtel, E. J. (1975) · Nature · doi:10.1038/253019a0 · Cited by 128
Hendsch, Z. S., & Tidor, B. (1999) · Protein Science · doi:10.1110/ps.8.7.1381 · Cited by 123
Rational Design of Helical Nanotubes from Self-Assembly of Coiled-Coil Lock Washers
Xu, C., Liu, R., Mehta, A. K., Guerrero-Ferreira, R., Wright, E. R., Dunin-Horkawicz, S., Morris, K. L., Serpell, L. C., Zuo, X., Wall, J. S., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4074529 · Cited by 123
Rosencwaig, A. (1978) · Advances in electronics and electron physics · doi:10.1016/s0065-2539(08)60413-8 · Cited by 117
The Structure and Topology of α-Helical Coiled Coils
Lupas, A. N., Baßler, J., & Dunin-Horkawicz, S. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-49674-0_4 · Cited by 126
Fraser, R., Furlong, D., Trus, B. L., Nibert, M. L., Fields, B. N., & Steven, A. C. (1990) · Journal of Virology · doi:10.1128/jvi.64.6.2990-3000.1990 · Cited by 115
Wood, C. W., Bruning, M., Ibarra, A. Á., Bartlett, G. J., Thomson, A. R., Sessions, R. B., Brady, R. L., & Woolfson, D. N. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu502 · Cited by 116
Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils
Woolfson, D. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104579 · Cited by 106
“The coiled coil came out of physics: Francis Crick ’ s description of the coiled coil, as he fi rst named it, is mathematical (22, 23).”
The structure of sodium thymonucleate fibres. II. The cylindrically symmetrical Patterson function
FRANKLIN, R. E., & Gosling, R. G. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001940 · Cited by 104
Duquerroy, S., Vigouroux, A., Rottier, P. J. M., Rey, F. A., & Bosch, B. (2005) · Virology · doi:10.1016/j.virol.2005.02.022 · Cited by 95
Coupling backbone flexibility and amino acid sequence selection in protein design
Su, A., & Mayo, S. L. (1997) · Protein Science · doi:10.1002/pro.5560060810 · Cited by 92
Gonzalez, L. C., Brown, R. A., Richardson, D., & Alber, T. (1996) · Nature Structural Biology · doi:10.1038/nsb1296-1002 · Cited by 89
Keating, A. E., Malashkevich, V. N., Tidor, B., & Kim, P. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261563398 · Cited by 86
Isolation and Characterization of the α Helical Regions of Epidermal Prekeratin
Skerrow, D., Matoltsy, A. G., & Matoltsy, M. N. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43739-3 · Cited by 84
Zhang, S., Kulp, D. W., Schramm, C. A., Mravic, M., Samish, I., & DeGrado, W. F. (2015) · Structure · doi:10.1016/j.str.2015.01.009 · Cited by 82
X-ray diffraction patterns of α-fibrous proteins
Fraser, R., MacRae, T. P., & Miller, A. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80193-0 · Cited by 80
Tertiary alphabet for the observable protein structural universe
Mackenzie, C. O., Zhou, J., & Grigoryan, G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607178113 · Cited by 72
The de novo design of α-helical peptides for supramolecular self-assembly
Beesley, J. L., & Woolfson, D. N. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2019.03.017 · Cited by 85
A coiled-coil motif that sequesters ions to the hydrophobic core
Hartmann, M. D., Ridderbusch, O., Zeth, K., Albrecht, R., Testa, O. D., Woolfson, D. N., Sauer, G., Dunin-Horkawicz, S., Lupas, A. N., & Alvarez, B. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907256106 · Cited by 82
Primary structure and sidechain interactions of PFL filamentous bacterial virus coat protein
NAKASHIMA, Y., Wiseman, R. L., Konigsberg, W. H., & Marvin, D. A. (1975) · Nature · doi:10.1038/253068a0 · Cited by 77
Adamovic, I., Mijailovich, S. M., & Karplus, M. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.122028 · Cited by 74
Towards functional de novo designed proteins
Dawson, W., Rhys, G. G., & Woolfson, D. N. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.06.011 · Cited by 71
The use of coiled-coil proteins in drug delivery systems
McFarlane, A. A., Orriss, G. L., & Stetefeld, J. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.05.034 · Cited by 70
Donald, J. E., Zhang, Y., Fiorin, G., Carnevale, V., Slochower, D. R., Gai, F., Klein, M. L., & DeGrado, W. F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019668108 · Cited by 69
Model-building studies of Inovirus: genetic variations on a geometric theme
Marvin, D. A. (1990) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(90)90064-h · Cited by 68
Design of two-stranded and three-stranded coiled-coil peptides
Betz, S., Fairman, R., O'Neil, K., Lear, J., & DeGrado, W. F. (1995) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1995.0048 · Cited by 66
Elasticity of α -Helical Coiled Coils
Wolgemuth, C. W., & Sun, S. X. (2006) · Physical Review Letters · doi:10.1103/physrevlett.97.248101 · Cited by 62
Tertiary templates for the design of diiron proteins
Summa, C. M., Lombardi, A., Lewis, M., & DeGrado, W. F. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80071-2 · Cited by 62
Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly
Taylor, K. C., Buvoli, M., Korkmaz, E. N., Buvoli, A. E., Zheng, Y., Heinze, N. T., Cui, Q., Leinwand, L. A., & Rayment, I. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505813112 · Cited by 61
Metadata
- Authors
- Crick, F. H. C.
- Corresponding author
- Crick, F. H. C.
- Venue
- Acta Crystallographica
- Published
- 1953-09-10
- Volume
- 6
- Issue
- 8
- Pages
- 685-689
- ISSN
- 0365-110X (ISSN-L)
- OpenAlex
- W2017774235
- Cited by
- 313
- References
- 0
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 9 · 2023: 9 · 2022: 11 · 2021: 7 · 2020: 7 · 2019: 12 · 2018: 7 · 2017: 15 · 2016: 9 · 2015: 5 · 2014: 5 · 2013: 3 · 2012: 8
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Acta Crystallographica (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › X-ray Diffraction in Crystallography
- Keywords
- coiled coil, Fourier transform, protein structure
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