In-cell nuclear magnetic resonance spectroscopy for studying intermolecular interactions
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.
Abstract
Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.
참고문헌 (35)
- Z. Serber, , Bioche mistry, 40, pp.14317~ (2001)
- Z. Serber, , J. Am. Chem. Soc, 123, pp.8895~ (2001)
- A. Reckel, , Chembiochem, 6, pp.1601~ (2005)
- H. Tochio, , Curr. Opin. Chem. Biol, 16, pp.609~ (2012)
- C. B. Kang, , Int. J. Mol. Sci, 20, pp.139~ (2019)
- T. Sugiki, , Expert Opin. Drug Discov, 9, pp.1189~ (2014)
- C. Barnes, , Proteins, 79, pp.347~ (2011)
- G. Xu, , Biochemistry, 53, pp.1971~ (2014)
- T. Ikeya, , Nat. Protoc, 5, pp.1051~ (2010)
- Y. Ito, , Methods Mol. Biol, 895, pp.19~ (2012)
- F. X. Theillet, , Chem. Rev, 114, pp.6661~ (2014)
- J. Danielsson, , Proc. Natl. Acad. Sci. USA, 112, pp.12402~ (2015)
- S. Majumder, , Biochemistry, 55, pp.4568~ (2016)
- J. Hamatsu, , J. Am. Chem. Soc, 135, pp.1688~ (2013)
- D. Sakakibara, , Nature, 458, pp.102~ (2009)
- K. Inomata, , Nature, 458, pp.106~ (2009)
- S. Ogino, , J. Am. Chem. Soc, 131, pp.10834~ (2009)
- L. Barbieri, , Nat. Protoc, 11, pp.1101~ (2016)
- F. X. Theillet, , Nature, 530, pp.45~ (2016)
- A. Binolfi, , Nat. Commun, 25, pp.10251~ (2016)
- S. Kubo, , Angew. Chem. Int. Ed. Engl, 52, pp.1208~ (2013)
- E. Luchinat, , Sci. Rep, 12, pp.17433~ (2017)
- E. Luchinat, , Acc. Chem. Res, 51, pp.1550~ (2018)
- Z. Serber, , J. Am. Chem. Soc, 126, pp.7119~ (2004)
- Z. Serber, , Nat. Protoc, 1, pp.2701~ (2006)
- S. Reckel, , Prog. Nucl. Magn. Reson. Spectrosc, 51, pp.91~ (2007)
- D. S. Burz, , Nat. Methods, 3, pp.91~ (2006)
- D. S. Burz, , Nat. Protoc, 1, pp.146~ (2006)
- J. Xue, , Adv. Exp. Med. Biol, 992, pp.17~ (2012)
- D. S. Burz, , Curr. Protoc. Protein Sci, 61, pp.1~ (2010)
- X. Mu, , Proc. Natl. Acad. Sci. USA, 114, pp.E4556~ (2017)
- J. Xie, , J. Med. Chem, 52, pp.3516~ (2009)
- S. Rahman, , Biochim. Biophys. Acta, 1865, pp.547~ (2017)
- C. M. DeMott, , ACS Chem. Biol, 13, pp.733~ (2018)
- T. Sugiki, , Molecules, 23, pp.E148~ (2018)
