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Protein Structural Ensembles Visualized by Solvent Paramagnetic Relaxation Enhancement
Author(s) -
Gong Zhou,
Gu XinHua,
Guo DaChuan,
Wang Jin,
Tang Chun
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201609830
Subject(s) - microsecond , protein dynamics , paramagnetism , molecular dynamics , relaxation (psychology) , chemical physics , protein structure , chemistry , characterization (materials science) , biological system , computational chemistry , biophysics , materials science , physics , nanotechnology , biology , biochemistry , quantum mechanics , astronomy , neuroscience
A protein can be in different conformations when fulfilling its function. Yet depiction of protein structural ensembles remains difficult. Here we show that the accurate measurement of solvent paramagnetic relaxation enhancement (sPRE) in the presence of an inert paramagnetic cosolute allows the assessment of protein dynamics. Demonstrated with two multi‐domain proteins, we present a method to characterize protein microsecond–millisecond dynamics based on the analysis of the sPRE. Provided with the known structures of a protein, our method uncovers an ensemble of structures that fully accounts for the observed sPRE. In conjunction with molecular dynamics simulations, our method can identify protein alternative conformation that has only been theorized before. Together, our method expands the application of sPRE beyond structural characterization of rigid proteins and complements the established PRE NMR technique.