NMR studies of large proteins
Publication date: Available online 17 July 2017
Source:Journal of Molecular Biology
Author(s): Yajun Jiang, Charalampos G. Kalodimos
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the Nuclear Magnetic Resonance (NMR) characterization of large protein systems with molecular weights of hundreds of kDa. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these developments by highlighting few cases that exemplify the uniqueness of NMR in providing atomic-resolution information into key dynamic processes and structures of protein complexes with high degree of flexibility.
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