Solution NMR spectroscopy for investigation of liquid-liquid phase separation
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Liquid-liquid phase separation (LLPS) of biomolecules, a newly-found phase behavior of molecules in the liquid phase, has shown to its relationship to various biological function and misfolding diseases. Extensive studies have increasingly revealed a general mechanism of LLPS and characterized the liquid droplet; however, intermolecular interactions of proteins and structural states of LLPS-inducing proteins inside of the droplet remain largely unknown. Solution NMR spectroscopy has emerged as a powerful approach as it provides invaluable information on protein intermolecular interactions and structures at the atomic and residue level. We herein comprehensively address useful techniques of solution NMR including the effect of paramagnetic relaxation enhancement for the study on the LLPS and droplet based on recent studies.
Abstract
Liquid-liquid phase separation (LLPS) of biomolecules, a newly-found phase behavior of molecules in the liquid phase, has shown to its relationship to various biological function and misfolding diseases. Extensive studies have increasingly revealed a general mechanism of LLPS and characterized the liquid droplet; however, intermolecular interactions of proteins and structural states of LLPS-inducing proteins inside of the droplet remain largely unknown. Solution NMR spectroscopy has emerged as a powerful approach as it provides invaluable information on protein intermolecular interactions and structures at the atomic and residue level. We herein comprehensively address useful techniques of solution NMR including the effect of paramagnetic relaxation enhancement for the study on the LLPS and droplet based on recent studies.
참고문헌 (23)
- S. Chong, , Science, 361 (2018)
- P. Li, , Nature, 483, pp.336~ (2012)
- W. Y. C. Huang, , Science, 363, pp.1098~ (2019)
- T. M. Franzmann, , Science, 359 (2018)
- M. Du, , Science, 361, pp.704~ (2018)
- M. Feric, , Cell, 165, pp.1686~ (2016)
- A. R. Strom, , Nature, 547, pp.241~ (2017)
- E. Boke, , Cell, 166, pp.637~ (2016)
- C. P. Brangwynne, , Science, 324, pp.1729~ (2009)
- A. Aguzzi, , Trends Cell Biol, 26, pp.547~ (2016)
- A. Patel, , Cell, 162, pp.1066~ (2015)
- M. Kato, , Cell, 149, pp.753~ (2012)
- D. T. Murray, , Cell, 171, pp.615~ (2017)
- K. A. Burke, , Mol. Cell, 60, pp.231~ (2015)
- A. C. Murthy, , Nat. Struct. Mol. Biol, 26, pp.637~ (2019)
- V. H. Ryan, , Mol. Cell, 69, pp.465~ (2018)
- T. Saio, , Biochim. Biophys. Acta. Gen. Subjects, 1864, pp.129332~ (2020)
- Toshihiko Sugiki, "Advanced techniques of solution nuclear magnetic resonance spectroscopy for structural investigation of protein-protein interaction", Journal of the Korean Magnetic Resonance Society, 22(4), pp.76~81 (2018), 한국자기공명학회[DOI]
- A.E. Conicella, , Structure, 24, pp.1537~ (2016)
- M. Clore, , Chem. Rev, 109, pp.4108~ (2009)
- S. Boeynaems, , Trends Cell Biol, 28, pp.420~ (2018)
- T. J. Nott, , Mol. Cell, 57, pp.936~ (2015)
- Clifford P. Brangwynne, , Nat. Phys, 11, pp.899~ (2015)
