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Protein dynamics in living cells studied by in‐cell NMR spectroscopy
Author(s) -
Li Conggang,
Liu Maili
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.12.023
Subject(s) - protein dynamics , nuclear magnetic resonance spectroscopy , dynamics (music) , biophysics , chemistry , cell function , protein function , protein structure , cell , biochemistry , physics , biology , stereochemistry , gene , acoustics
Most proteins function in cells where protein concentrations can reach 400 g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in‐cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been characterized by in‐cell NMR, and then discuss the remaining challenges and future directions.