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Weak and Transient Protein Interactions Determined by Solid‐State NMR
Author(s) -
Dannatt Hugh R. W.,
Felletti Michele,
Jehle Stefan,
Wang Yao,
Emsley Lyndon,
Dixon Nicholas E.,
Lesage Anne,
Pintacuda Guido
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201511609
Subject(s) - solid state nuclear magnetic resonance , macromolecule , magic angle spinning , chemistry , nuclear magnetic resonance spectroscopy , chemical physics , molecule , nmr spectra database , chemical shift , crystallography , relaxation (psychology) , transverse relaxation optimized spectroscopy , molecular dynamics , nuclear magnetic resonance spectroscopy of nucleic acids , fluorine 19 nmr , nuclear magnetic resonance , computational chemistry , spectral line , stereochemistry , physics , organic chemistry , biochemistry , psychology , social psychology , astronomy
Despite their roles in controlling many cellular processes, weak and transient interactions between large structured macromolecules and disordered protein segments cannot currently be characterized at atomic resolution by X‐ray crystallography or solution NMR. Solid‐state NMR does not suffer from the molecular size limitations affecting solution NMR, and it can be applied to molecules in different aggregation states, including non‐crystalline precipitates and sediments. A solid‐state NMR approach based on high magnetic fields, fast magic‐angle sample spinning, and deuteration provides chemical‐shift and relaxation mapping that enabled the characterization of the structure and dynamics of the transient association between two regions in an 80 kDa protein assembly. This led to direct verification of a mechanism of regulation of E. coli DNA metabolism.