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When Small becomes Too Big: Expanding the Use of In‐Cell Solid‐State NMR Spectroscopy
Author(s) -
Narasimhan Siddarth,
Folkers Gert E.,
Baldus Marc
Publication year - 2020
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.202000167
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , context (archaeology) , solid state nuclear magnetic resonance , spectroscopy , intermolecular force , nanotechnology , biophysics , chemical physics , nuclear magnetic resonance , molecule , physics , stereochemistry , materials science , organic chemistry , paleontology , quantum mechanics , biology
Abstract Solution‐state NMR spectroscopy has become a powerful tool to study soluble proteins in cells, provided that they tumble sufficiently fast. In addition, cryo‐electron tomography (cryo‐ET) has recently displayed a tremendous potential to probe structures of large proteins and assemblies in their native cellular environments. However, challenges remain to obtain atomic‐level information in native cell settings for proteins that are small, disordered, or are strongly engaged in intermolecular interactions. In this Minireview, we discuss recent progress in using sensitivity enhanced solid‐state NMR spectroscopy methods in the context of cellular structural biology.