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Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry
Open accessAbstract
Motions in biomolecules are critical for biochemical reactions. In cells, many biochemical reactions are executed inside of biomolecular condensates formed by ultradynamic intrinsically disordered proteins. A deep understanding of the conformational dynamics of intrinsically disordered proteins in biomolecular condensates is therefore of utmost importance but is complicated by diverse obstacles. Here we review emerging data on the motions of intrinsically disordered proteins inside of liquidlike condensates. We discuss how liquid-liquid phase separation modulates internal motions across a wide range of time and length scales. We further highlight the importance of intermolecular interactions that not only drive liquid-liquid phase separation but appear as key determinants for changes in biomolecular motions and the aging of condensates in human diseases. The review provides a framework for future studies to reveal the conformational dynamics of intrinsically disordered proteins in the regulation of biomolecular condensate chemistry.
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“Disordered proteins (regions) are characterized by broad and heterogeneous ensembles where the differences in the relative conformational stabilities are small, or even minor and the barriers are low.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [127]
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Items 201–257 of 257
Palmer, A. G. I., & Koss, H. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.028 · Cited by 81
Test and Evaluation of ff99IDPs Force Field for Intrinsically Disordered Proteins
Ye, W., Ji, D., Wang, W., Luo, R., & Chen, H. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00043 · Cited by 80
Kalwarczyk, T., Sozański, K., Ochab-Marcinek, A., Szymański, J., Tabaka, M., Hou, S., & Hołyst, R. (2015) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2015.06.007 · Cited by 78
Adamski, W., Salvi, N., Maurin, D., Magnat, J., Milles, S., Jensen, M. R., Abyzov, A., Moreau, C., & Blackledge, M. J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b09002 · Cited by 75
Self-citationPhoton Statistics and Dynamics of Fluorescence Resonance Energy Transfer
Berglund, A. J., Doherty, A. C., & Mabuchi, H. (2002) · Physical Review Letters · doi:10.1103/physrevlett.89.068101 · Cited by 74
Gill, M. L., Byrd, R. A., & Palmer, A. G. I. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp06197k · Cited by 72
Cho, M., Kim, H., Bernadó, P., Fernández, C. O., Blackledge, M. J., & Zweckstetter, M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja067482k · Cited by 71
Self-citationSeparation of the rotational contribution in fluorescence correlation experiments
Kask, P., Piksarv, P., Pooga, M., Mets, Ü., & Lippmaa, E. (1989) · Biophysical Journal · doi:10.1016/s0006-3495(89)82796-1 · Cited by 69
Physical Chemistry of Cellular Liquid‐Phase Separation
Bentley, E. P., Frey, B. B., & Deniz, A. A. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201805093 · Cited by 67
König, I., Soranno, A., Nettels, D., & Schuler, B. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202016804 · Cited by 62
Salvi, N., Abyzov, A., & Blackledge, M. J. (2017) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2017.06.001 · Cited by 61
Self-citationBiophysical studies of phase separation integrating experimental and computational methods
Fawzi, N. L., Parekh, S. H., & Mittal, J. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.04.004 · Cited by 59
Ramis, R., Ortega‐Castro, J., Casasnovas, R., Mariño, L., Vilanova, B., Adrover, M., & Frau, J. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00921 · Cited by 58
Choi, J., & Pappu, R. V. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b00573 · Cited by 56
Xue, Y., & Skrynnikov, N. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja201605c · Cited by 55
Chen, J., Zaer, S., Drori, P., Zamel, J., Joron, K., Kalisman, N., Lerner, E., & Dokholyan, N. V. (2021) · Structure · doi:10.1016/j.str.2021.05.002 · Cited by 55
Lum, J. K., Neuweiler, H., & Fersht, A. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2078619 · Cited by 54
Looking at the Disordered Proteins through the Computational Microscope
Das, P., Matysiak, S., & Mittal, J. (2018) · ACS Central Science · doi:10.1021/acscentsci.7b00626 · Cited by 53
Tang, W. S., Fawzi, N. L., & Mittal, J. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c07545 · Cited by 53
Haenni, D., Zosel, F., Reymond, L., Nettels, D., & Schuler, B. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp402352s · Cited by 52
Liu, B., Chia, D., Csizmók, V., Farber, P. J., Forman-Kay, J. D., & Gradinaru, C. C. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp500776v · Cited by 50
Scanning FCS for the Characterization of Protein Dynamics in Live Cells
Petrášek, Z., Ries, J., & Schwille, P. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)72005-x · Cited by 49
Gomes, G.-N. W., & Gradinaru, C. C. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.06.008 · Cited by 46
Yuwen, T., Brady, J. P., & Kay, L. E. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09576 · Cited by 46
Sauer, M., & Neuweiler, H. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-649-8_27 · Cited by 45
Nasir, I., Onuchic, P. L., Labra, S. R., & Deniz, A. A. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.04.007 · Cited by 43
Biomolecular condensation of the microtubule-associated protein tau
Ukmar, T., Wegmann, S., & Zweckstetter, M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.06.007 · Cited by 41
Self-citationPicosecond fluorescence studies of polypeptide dynamics: fluorescence anisotropies and lifetimes
Chen, L. X., Petrich, J. W., Fleming, G. R., & Perico, A. (1987) · Chemical Physics Letters · doi:10.1016/0009-2614(87)80150-1 · Cited by 40
Cousin, S. F., Kadeřávek, P., Bolik-Coulon, N., Gu, Y.-N., Charlier, C., Carlier, L., Bruschweiler-Li, L., Marquardsen, T., Tyburn, J.-M., Brüschweiler, R., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09107 · Cited by 39
Fold recognition and accurate query-template alignment by a combination of PSI-BLAST and threading
Shan, Y., Wang, G., & Zhou, H. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010101)42:1 · Cited by 38
Modig, K., & Poulsen, F. M. (2008) · Journal of Biomolecular NMR · doi:10.1007/s10858-008-9280-0 · Cited by 38
Pieper, C., & Enderlein, J. (2011) · Chemical Physics Letters · doi:10.1016/j.cplett.2011.06.091 · Cited by 38
Wang, Z., Pisano, S., Ghini, V., Kadeřávek, P., Zachrdla, M., Pelupessy, P., Kazmierczak, M., Marquardsen, T., Tyburn, J., Bouvignies, G., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c01388 · Cited by 37
Manger, L. H., Foote, A. K., Wood, S. L., Holden, M. R., Heylman, K. D., Margittai, M., & Goldsmith, R. H. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201708242 · Cited by 36
HyRes: a coarse-grained model for multi-scale enhanced sampling of disordered protein conformations
Liu, X., & Chen, J. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp06736d · Cited by 36
Shayegan, M., Tahvildari, R., Metera, K., Kisley, L., Michnick, S. W., & Leslie, S. R. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13349 · Cited by 35
Wang, A., Zhang, Z., & Li, G. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b03471 · Cited by 31
Predicting the Rotational Tumbling of Dynamic Multidomain Proteins and Supramolecular Complexes
Rezaei‐Ghaleh, N., Klama, F., Munari, F., & Zweckstetter, M. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201305094 · Cited by 30
Self-citationVáradi, M., & Tompa, P. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_11 · Cited by 30
Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins
Jain, N., Narang, D., Bhasne, K., Dalal, V., Arya, S., Bhattacharya, M., & Mukhopadhyay, S. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.07.023 · Cited by 30
Prompers, J. J., Scheurer, C., & Brüschweiler, R. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4353 · Cited by 29
Pan, Q., Sun, D., Xue, J., Hao, J., Zhao, H., Lin, X., Yu, L., & He, Y. (2020) · ACS Nano · doi:10.1021/acsnano.0c05486 · Cited by 28
NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins
Kurzbach, D., Kontaxis, G., Coudevylle, N., & Konrat, R. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_5 · Cited by 27
Bolik-Coulon, N., Kadeřávek, P., Pelupessy, P., Dumez, J., Ferrage, F., & Cousin, S. F. (2020) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2020.106718 · Cited by 27
Ochsenbein, F., Guérois, R., Neumann, J., Sanson, A., Guittet, É., & van Heijenoort, C. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1008390606077 · Cited by 25
Song, D., Jo, Y., Choi, J., & Jung, Y. (2020) · Nature Communications · doi:10.1038/s41467-020-19476-4 · Cited by 25
Ochsenbein, F., Neumann, J., Guittet, É., & van Heijenoort, C. (2002) · Protein Science · doi:10.1110/ps.4000102 · Cited by 24
Amorós, D., Ortega, Á., & de la Torre, J. G. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct300948u · Cited by 24
Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters
Kragelj, J., Blackledge, M. J., & Jensen, M. R. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_4 · Cited by 22
Self-citationThe effects of individual amino acids on the fast folding dynamics of α-helical peptides
Gooding, E. A., Ramajo, A. P., Wang, J., Palmer, C., Fouts, E., & Völk, M. (2005) · Chemical Communications · doi:10.1039/b511072f · Cited by 20
König, I., Soranno, A., Nettels, D., & Schuler, B. (2021) · Angewandte Chemie · doi:10.1002/ange.202016804 · Cited by 18
Biomolecular phase separation through the lens of sodium‐23 NMR
Fuentes‐Monteverde, J. C., Becker, S., & Rezaei‐Ghaleh, N. (2020) · Protein Science · doi:10.1002/pro.4010 · Cited by 17
Viegas, A., Dollinger, P., Verma, N., Kubiak, J., Viennet, T., Seidel, C. A. M., Gohlke, H., Etzkorn, M., Kovačić, F., & Jaeger, K. (2020) · Scientific Reports · doi:10.1038/s41598-020-60093-4 · Cited by 16
Rezaei‐Ghaleh, N., Munari, F., Becker, S., Assfalg, M., & Griesinger, C. (2019) · Chemical Communications · doi:10.1039/c9cc06124j · Cited by 15
Rezaei‐Ghaleh, N., Klama, F., Munari, F., & Zweckstetter, M. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu824 · Cited by 10
Self-citationKimmich, R., & Anoardo, E. (2004) · ChemInform · doi:10.1002/chin.200447278 · Cited by 8
Manger, L. H., Foote, A. K., Wood, S. L., Holden, M. R., Heylman, K. D., Margittai, M., & Goldsmith, R. H. (2017) · Angewandte Chemie · doi:10.1002/ange.201708242 · Cited by 4
Flagged first, then by citations
2 of the 259 references couldn’t be matched to a known paper.
Research works printed but not linked: 7
- Valentin G., 1836, Repertorium für Anatomie und Physiologie: kritische Darstellung fremder und Ergebnisse eigener Forschung
- Wagner R., 1835, Arch. Anat. Physiol. wiss. Med. Müllers Archiv., 268, 373
- Cajal S. R., 1903, Trab. Lab. Invest. Biol. Univ. Madrid, 2, 129
- Gunton, J. D.; San Miguel, M.; Sahni, P. S. The Dynamics of First Order Phase Transitions. In Phase Transitions and Critical Phenomena; Domb, C., Lebowitz, J. L., Eds. Academic: New York, 1983; Vol. 8, pp 269–482.
- Kowalewski, J.; Maler, L. Nuclear Spin Relaxation in Liquids: Theory, Experiments, and Applications, 2nd ed. CRC Press, 2017; pp 118–119.
- Rubinstein M., 1997, Trends Polym. Sci., 6, 181
- 10.1038/npre.2010.4422.1 · DOI · Paper page
Cited by
Sorted by citations
AlphaFold, Artificial Intelligence (AI), and Allostery
Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190
Learning the chemical grammar of biomolecular condensates
Kilgore, H. R., & Young, R. A. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01046-y · Cited by 174
Micropolarity governs the structural organization of biomolecular condensates
Ye, S., Latham, A. P., Tang, Y., Hsiung, C., Chen, J., Luo, F., Liu, Y., Zhang, B., & Zhang, X. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01477-1 · Cited by 144
The role of biomolecular condensates in protein aggregation
Visser, B. S., Lipiński, W. P., & Spruijt, E. (2024) · Nature Reviews Chemistry · doi:10.1038/s41570-024-00635-w · Cited by 142
Principles Governing the Phase Separation of Multidomain Proteins
Mohanty, P., Kapoor, U., Devarajan, D. S., Phan, T. M., Rizuan, A., & Mittal, J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00210 · Cited by 119
Metadata
- Authors
- Abyzov, A., Blackledge, M., & Zweckstetter, M.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Zweckstetter, Markus
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2022-02-18
- Volume
- 122
- Issue
- 6
- Pages
- 6719-6748
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC8949871
- OpenAlex
- W4212888384
- Cited by
- 215
- References
- 259
- Citations by year
- 2026: 44 · 2025: 63 · 2024: 60 · 2023: 35 · 2022: 13
- FWCI
- 4.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Chemical Reviews (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- DZNE Pub (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 860/B02, SPP2191, ZW 71/9-1)
- H2020 European Research Council (787679)
- Volkswagen Foundation (AZ 98188)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- intrinsically disordered proteins, biomolecular condensates, conformational dynamics, liquid-liquid phase separation, intermolecular interactions
- MeSH terms
- Biomolecular Condensates, Humans, Molecular Conformation, Intrinsically Disordered Proteins
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