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Broadband Dynamics of Ubiquitin by Anionic and Cationic Nanoparticle Assisted NMR Spin Relaxation
Author(s) -
Wardenfelt Stacey,
Xiang Xinyao,
Xie Mouzhe,
Yu Lei,
BruschweilerLi Lei,
Brüschweiler Rafael
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202007205
Subject(s) - nanosecond , relaxation (psychology) , picosecond , protein dynamics , ubiquitin , microsecond , chemical physics , nanoparticle , chemistry , molecular dynamics , dynamics (music) , cationic polymerization , nuclear magnetic resonance spectroscopy , biophysics , materials science , computational chemistry , nanotechnology , physics , stereochemistry , polymer chemistry , biochemistry , psychology , social psychology , laser , astronomy , acoustics , optics , gene , biology
Abstract The quantitative and comprehensive description of the internal dynamics of proteins is critical for understanding their function. Nanoparticle‐assisted 15 N NMR spin relaxation spectroscopy is a new method for the observation of picosecond to microsecond dynamics of proteins when transiently interacting with the surface of the nanoparticles (NPs). The method is applied here to the protein ubiquitin in the presence of anionic and cationic silica NPs (SNPs) of different sizes. The backbone dynamics profiles are reproducible and strikingly similar to each other, indicating that specific protein–SNP interactions are unimportant. The dynamics profiles closely match the sub‐nanosecond dynamics S 2 values observed by model‐free analysis of standard 15 N relaxation of ubiquitin in free solution, indicating that the bulk of the ubiquitin backbone dynamics in solution is confined to sub‐nanosecond timescales and, hence, it is dynamically more restrained than previous NMR studies have suggested.