Does Intrinsic Disorder in Proteins Favor Their Interaction with Lipids?
Abstract
Intrinsically disordered proteins (IDPs) are implicated in a range of human diseases, some of which are associated with the ability to bind to lipids. Although the presence of solvent‐exposed hydrophobic regions in IDPs should favor their interactions with low‐molecular‐weight hydrophobic/amphiphilic compounds, this hypothesis has not been systematically explored as of yet. In this study, the analysis of the DisProt database with regard to the presence of lipid‐binding IDPs (LBIDPs) reveals that they comprise, at least, 15% of DisProt entries. LBIDPs are classified into four groups by ligand type, functional categories, domain structure, and conformational state. 57% of LBIDPs are classified as ordered according to the CH‐CDF analysis, and 70% of LBIDPs possess lengths of disordered regions below 50%. To investigate the lipid‐binding properties of IDPs for which lipid binding is not reported, three proteins from different conformational groups are rationally selected. They all are shown to bind linoleic (LA) and oleic (OA) acids with capacities ranging from 9 to 34 LA/OA molecules per protein molecule. The association with LA/OA causes the formation of high‐molecular‐weight lipid–protein complexes. These findings suggest that lipid binding is common among IDPs, which can favor their involvement in lipid metabolism.
Integrity signals
Registry
Cites
Statistics
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?
15% of all disordered proteins bind lipid.
“it is perhaps not surprising that 15% of all disordered proteins bind lipid [288, 289].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [288]
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,694 · see citing works
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · see citing works
How to measure and predict the molar absorption coefficient of a protein
Pace, C., Vajdos, F., Fee, L. R., Grimsley, G., & Gray, T. (1995) · Protein Science · doi:10.1002/pro.5560041120 · Cited by 3,924 · see citing works
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272 · see citing works
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,469 · see citing works
A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · see citing works
Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,406 · see citing works
Self-citationUnderstanding protein non-folding
Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,188 · see citing works
Self-citationNeurodegenerative Diseases and Prions
Prusiner, S. B. (2001) · New England Journal of Medicine · doi:10.1056/nejm200105173442006 · Cited by 767 · see citing works
Fink, A. L. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.01.002 · Cited by 700 · see citing works
Comparing and Combining Predictors of Mostly Disordered Proteins
Oldfield, C. J., Cheng, Y., Cortese, M. S., Brown, C. J., Uversky, V. N., & Dunker, A. K. (2005) · Biochemistry · doi:10.1021/bi047993o · Cited by 544 · see citing works
Self-citationIntrinsically disordered proteins from A to Z
Uversky, V. N. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.001 · Cited by 434 · see citing works
Self-citationTOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder
Campen, A., Williams, R. M., Brown, C. J., Meng, J., Uversky, V. N., & Dunker, A. K. (2008) · Protein and Peptide Letters · doi:10.2174/092986608785849164 · Cited by 422 · see citing works
Self-citationStructure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M. A., Tidow, H., Rutherford, T. J., Markwick, P. R. L., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M. J., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 420 · see citing works
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
van der Goot, F. G., González‐Mañas, J. M., Lakey, J. H., & Pattus, F. (1991) · Nature · doi:10.1038/354408a0 · Cited by 418 · see citing works
Alzheimer's disease in Down's syndrome: Clinicopathologic studies
Wisniewski, K. E., Dalton, A. J., McLachlan, D. R. C., Wen, G. Y., & Wisniewski, H. M. (1985) · Neurology · doi:10.1212/wnl.35.7.957 · Cited by 417 · see citing works
Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins
Kovács, D., Kalmár, É., Török, Z., & Tompa, P. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.118208 · Cited by 390 · see citing works
Self-citation(1997) · Europe PMC (PubMed Central) · Cited by 354 · see citing works
The PROSITE dictionary of sites and patterns in proteins, its current status
Bairoch, A. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.13.3097 · Cited by 350 · see citing works
DisProt 7.0: a major update of the database of disordered proteins
Piovesan, D., Tabaro, F., Mičetić, I., Necci, M., Quaglia, F., Oldfield, C. J., Aspromonte, M. C., Davey, N. E., Davidović, R. S., Dosztányi, Z., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1056 · Cited by 288 · see citing works
Self-citationCFTR regulatory region interacts with NBD1 predominantly via multiple transient helices
Baker, J. M., Hudson, R. P., Kanelis, V., Choy, W., Thibodeau, P. H., Thomas, P., & Forman-Kay, J. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1278 · Cited by 280 · see citing works
The role of lipid–protein interactions in amyloid-type protein fibril formation
Gorbenko, G. P., & Kinnunen, P. K. J. (2006) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2006.02.006 · Cited by 267 · see citing works
Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
Dev, K. K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 262 · see citing works
Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro
Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 244 · see citing works
Alpha-synuclein, lipids and Parkinson’s disease
Ruipérez, V., Darios, F. D., & Davletov, B. A. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.05.004 · Cited by 233 · see citing works
Covalent lipid modifications of proteins
Resh, M. D. (2013) · Current Biology · doi:10.1016/j.cub.2013.04.024 · Cited by 231 · see citing works
Potential of Casein as a Carrier for Biologically Active Agents
Głąb, T. K., & Boratyński, J. (2017) · Topics in Current Chemistry · doi:10.1007/s41061-017-0158-z · Cited by 231 · see citing works
Raft lipids as common components of human extracellular amyloid fibrils
Gellermann, G. P., Appel, T. R., Tannert, A., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407035102 · Cited by 207 · see citing works
Abundance of Intrinsic Disorder in Protein Associated with Cardiovascular Disease
Cheng, Y., LeGall, T., Oldfield, C. J., Dunker, A. K., & Uversky, V. N. (2006) · Biochemistry · doi:10.1021/bi060981d · Cited by 203 · see citing works
Self-citationA majority of the cancer/testis antigens are intrinsically disordered proteins
Rajagopalan, K., Mooney, S. M., Parekh, N., Getzenberg, R. H., & Kulkarni, P. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23252 · Cited by 188 · see citing works
Differential Assembly of Human Tau Isoforms in the Presence of Arachidonic Acid
King, M. E., Gamblin, T. C., Kuret, J., & Binder, L. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741749.x · Cited by 179 · see citing works
Mark, W.-Y., Liao, J. C. C., Lü, Y., Ayed, A., Laister, R. C., Szymczyna, B. R., Chakrabartty, A., & Arrowsmith, C. H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.045 · Cited by 175 · see citing works
Secondary structure of bovine αS1- and β-casein in solution
Creamer, L. K., Richardson, T., & Parry, D. A. D. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90505-1 · Cited by 167 · see citing works
Diphtheria toxin: membrane interaction and membrane translocation
London, E. (1992) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(92)90033-7 · Cited by 155 · see citing works
Oxidative Regulation of Fatty Acid-Induced Tau Polymerization
Gamblin, T. C., King, M. E., Kuret, J., Berry, R. W., & Binder, L. I. (2000) · Biochemistry · doi:10.1021/bi001876l · Cited by 151 · see citing works
Protein disorder—a breakthrough invention of evolution?
Schlessinger, A., Schaefer, C. A., Vicedo, E., Schmidberger, M., Punta, M., & Rost, B. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.014 · Cited by 147 · see citing works
Comparative properties of vertebrate parvalbumins.
Blum, H. E., Lehky, P., Kohler, L., et al. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40438-8 · Cited by 143 · see citing works
Klein, T. R., Kirsch, D., KAUFMANN, R. L., & Riesner, D. (1998) · Biological Chemistry · doi:10.1515/bchm.1998.379.6.655 · Cited by 143 · see citing works
Xue, B., Oldfield, C. J., Dunker, A. K., & Uversky, V. N. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.070 · Cited by 142 · see citing works
Self-citationFatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us
Hamilton, J. A. (2003) · Progress in Lipid Research · doi:10.1016/j.plipres.2003.09.002 · Cited by 142 · see citing works
Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease
Adegbuyiro, A., Sedighi, F., Pilkington, A. W., Groover, S. E., & Legleiter, J. A. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b00936 · Cited by 141 · see citing works
Uversky, V. N., Roman, A., Oldfield, C. J., & Dunker, A. K. (2006) · Journal of Proteome Research · doi:10.1021/pr0602388 · Cited by 138 · see citing works
Self-citationPatil, S. P., & Chan, C. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.05.003 · Cited by 138 · see citing works
Lipid binding domains: more than simple lipid effectors
Stahelin, R. V. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800078-jlr200 · Cited by 127 · see citing works
Portnaya, I., Cogan, U., Livney, Y. D., et al. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf060119c · Cited by 125 · see citing works
Castagné, N., Barbier, A., Bernard, J., et al. (2004) · Journal of General Virology · doi:10.1099/vir.0.79830-0 · Cited by 118 · see citing works
Interactions of the carboxyl group of oleic acid with bovine serum albumin: a 13C NMR study.
Parks, J. S., Cistola, D. P., SMALL, D. M., et al. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44661-8 · Cited by 108 · see citing works
Polyglutamine diseases: protein cleavage and aggregation
Zoghbi, H. Y., & Orr, H. T. (1999) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(99)00013-6 · Cited by 107 · see citing works
Polyunsaturated Fatty Acids Induce α-Synuclein-Related Pathogenic Changes in Neuronal Cells
Assayag, K., Yakunin, E., Loeb, V., Selkoe, D. J., & Sharon, R. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070373 · Cited by 106 · see citing works
Ng, K. P., Potikyan, G., Savene, R. O. V., Denny, C. T., Uversky, V. N., & Lee, K. A. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607007104 · Cited by 102 · see citing works
Self-citationAberrant Phosphorylation of α-Synuclein in Human Niemann-Pick Type C1 Disease
Saito, Y., Suzuki, K., Hulette, C. M., & Murayama, S. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.4.323 · Cited by 97 · see citing works
Cistola, D. P., SMALL, D. M., & Hamilton, J. A. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60914-7 · Cited by 91 · see citing works
Who Is Mr. HAMLET? Interaction of Human α-Lactalbumin with Monomeric Oleic Acid
Knyazeva, E. L., Grishchenko, V. M., Фадеев, Р. С., Акатов, В. С., Permyakov, S. E., & Permyakov, E. A. (2008) · Biochemistry · doi:10.1021/bi801423s · Cited by 82 · see citing works
Self-citationMalaney, P., Pathak, R. R., Xue, B., Uversky, V. N., & Davé, V. (2013) · Scientific Reports · doi:10.1038/srep02035 · Cited by 79 · see citing works
Self-citationThe amino acid sequence of the calmodulin obtained from sea anemone (Metridium senile) muscle
Takagi, T., Nemoto, T., Konishi, K., et al. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91225-5 · Cited by 74 · see citing works
Škrabana, R., Ševčı́k, J., & Novák, M. (2006) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-006-9083-3 · Cited by 72 · see citing works
Thermal and Alkaline Denaturation of Bovine β-Casein
Qi, P. X., Wickham, E. D., & Farrell, H. M. (2004) · The Protein Journal · doi:10.1023/b:jopc.0000039553.66233.3f · Cited by 59 · see citing works
Critical Scaffolding Regions of the Tumor Suppressor Axin1 Are Natively Unfolded
Noutsou, M., Duarte, A. M. S., Anvarian, Z., Didenko, T., Minde, D. P., Kuper, I., de Ridder, I., Oikonomou, C., Friedler, A., Boelens, R., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.11.013 · Cited by 58 · see citing works
Minde, D., Radli, M., Forneris, F., Maurice, M. M., & Rüdiger, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077257 · Cited by 57 · see citing works
Apo‐parvalbumin as an intrinsically disordered protein
Permyakov, S. E., Bakunts, A. G., Denesyuk, A. I., Knyazeva, E. L., Uversky, V. N., & Permyakov, E. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21974 · Cited by 56 · see citing works
Self-citationCasu, F., Duggan, B. M., & Hennig, M. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.07.022 · Cited by 53 · see citing works
Lee, Y. J., Wang, S., Slone, S. R., Yacoubian, T. A., & Witt, S. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015946 · Cited by 50 · see citing works
Llorente, M. T., Taylor, I. A., López‐Viñas, E., et al. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21988 · Cited by 50 · see citing works
A new large-scale purification procedure for muscular parvalbumins
Haiech, J., Derancourt, J., Péchère, J.-F., et al. (1979) · Biochimie · doi:10.1016/s0300-9084(79)80155-8 · Cited by 49 · see citing works
The Roles of Intrinsic Disorder in Orchestrating the Wnt-Pathway
Xue, B., Dunker, A. K., & Uversky, V. N. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/073911012010525024 · Cited by 49 · see citing works
Self-citationStochastic machines as a colocalization mechanism for scaffold protein function
Xue, B., Romero, P. R., Noutsou, M., Maurice, M. M., Rüdiger, S. G. D., William, A. M., Mizianty, M. J., Kurgan, L., Uversky, V. N., & Dunker, A. K. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.006 · Cited by 47 · see citing works
Self-citationA Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes
Du, Z., & Uversky, V. N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102010 · Cited by 46 · see citing works
Self-citationA novel method for preparation of HAMLET-like protein complexes
Permyakov, S. E., Knyazeva, E. L., Leonteva, M. V., Фадеев, Р. С., Chekanov, A. V., Zhadan, A. P., Håkansson, A., Акатов, В. С., & Permyakov, E. A. (2011) · Biochimie · doi:10.1016/j.biochi.2011.05.002 · Cited by 41 · see citing works
Self-citationInterleukin-11 binds specific EF-hand proteins via their conserved structural motifs
Kazakov, A. S., Sokolov, A. S., Vologzhannikova, A. A., et al. (2016) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1132392 · Cited by 33 · see citing works
Influence of Monovalent Cations on Rat α- and β-Parvalbumin Stabilities
Henzl, M. T., Larson, J. D., & Agah, S. (2000) · Biochemistry · doi:10.1021/bi992762g · Cited by 33 · see citing works
Stability and Solvent Accessibility of SecA Protein of Escherichia coli
Song, M., & Kim, H. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021840 · Cited by 28 · see citing works
Panja, S., Khatua, D. K., & Halder, M. (2018) · ACS Omega · doi:10.1021/acsomega.7b01741 · Cited by 28 · see citing works
Metal-controlled interdomain cooperativity in parvalbumins
Permyakov, S. E., Bakunts, A. G., Permyakova, M. E., Denesyuk, A. I., Uversky, V. N., & Permyakov, E. A. (2009) · Cell Calcium · doi:10.1016/j.ceca.2009.07.001 · Cited by 26 · see citing works
Self-citationAssembly In Vitro of Tau Protein and its Implications in Alzheimers Disease
Ávila, J., Pérez, M., Lucas, J. J., et al. (2004) · Current Alzheimer Research · doi:10.2174/1567205043332207 · Cited by 24 · see citing works
The lipid content of amyloid fibrils purified by a variety of methods.
Kim, I. C., Shirahama, T., & Cohen, A. S. (1967) · PubMed · Cited by 24 · see citing works
Rao, K. S. P. B., & Gerday, C. (1973) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(73)90242-3 · Cited by 18 · see citing works
Ea, P., Di, K., Lp, K., et al. (1988) · PubMed · Cited by 15 · see citing works
Rao, K. S. P. B., & Gerday, C. (1973) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(73)90264-2 · Cited by 14 · see citing works
Леонидовна, Н. Е., Kazakov, A. S., Khasanova, L. M., Permyakov, E. A., & Permyakov, S. E. (2013) · Biochemistry · doi:10.1021/bi400643s · Cited by 14 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Intrinsically disordered proteins play diverse roles in cell signaling
Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222 · see citing works
Self-citationIntrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?
Cornish, J., Chamberlain, S. G., Owen, D., & Mott, H. R. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200467 · Cited by 69 · see citing works
- Authors
- Deryusheva, E., Nemashkalova, E., Galloux, M., Richard, C., Eléouët, J., Kovacs, D., Van Belle, K., Tompa, P., Uversky, V., & Permyakov, S.
- Affiliations
- Russian Academy of Sciences (RU)
- Russian Academy of Sciences Institute for Biological Instrumentation Pushchino Moscow Region 142290 Russia
- Université Paris-Saclay (FR)
- VIM, INRA Université Paris‐Saclay Jouy‐en‐Josas 78350 France
- Vrije Universiteit Brussel (BE)
- VIB, Structural Biology Research Center Vrije Universiteit Brussel Brussels 1050 Belgium
- Corresponding author
- Deryusheva, Evgenia
- Permyakov, Sergei
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2019-01-25
- Volume
- 19
- Issue
- 6
- Pages
- e1800098-e1800098
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W2908266160
- Cited by
- 34
- References
- 81
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 6 · 2023: 4 · 2022: 2 · 2021: 8 · 2020: 3 · 2019: 1
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- PROTEOMICS (publishedVersion)
- PubMed (publishedVersion)
- Repository of the Academy's Library (Library of the Hungarian Academy of Sciences) (acceptedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- HAL (submittedVersion)
- Funders
- Russian Foundation for Basic Research (16‐34‐00744,)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- intrinsically disordered proteins, lipid binding, protein-lipid interactions, linoleic acid, oleic acid, hydrophobic region, conformational states, lipid-protein complexes, lipid metabolism
- MeSH terms
- Animals, Fatty Acids, Humans, Protein Binding, Protein Structure, Quaternary, Databases, Protein, Proteomics, Lipid Metabolism, Intrinsically Disordered Proteins
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
