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The Role of Rotational Motion in Diffusion NMR Experiments on Supramolecular Assemblies: Application to Sup35NM Fibrils
Author(s) -
Kharkov Boris B.,
Podkorytov Ivan S.,
Bondarev Stanislav A.,
Belousov Mikhail V.,
Salikov Vladislav A.,
Zhouravleva Galina A.,
Skrynnikov Nikolai R.
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.202102408
Subject(s) - supramolecular chemistry , pulsed field gradient , rotational diffusion , fibril , diffusion , biomolecule , chemistry , micrometer , chemical physics , characterization (materials science) , crystallography , nanotechnology , materials science , molecule , physics , organic chemistry , thermodynamics , biochemistry , optics , crystal structure
Pulsed‐field gradient (PFG) NMR is an important tool for characterization of biomolecules and supramolecular assemblies. However, for micrometer‐sized objects, such as amyloid fibrils, these experiments become difficult to interpret because in addition to translational diffusion they are also sensitive to rotational diffusion. We have constructed a mathematical theory describing the outcome of PFG NMR experiments on rod‐like fibrils. To test its validity, we have studied the fibrils formed by Sup35NM segment of the prion protein Sup35. The interpretation of the PFG NMR data in this system is fully consistent with the evidence from electron microscopy. Contrary to some previously expressed views, the signals originating from disordered regions in the fibrils can be readily differentiated from the similar signals representing small soluble species (e.g. proteolytic fragments). This paves the way for diffusion‐sorted NMR experiments on complex amyloidogenic samples.