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Comparative study of REDOR and CPPI derived order parameters by 1H-detected MAS NMR and MD simulations.
J. Phys. Chem. B 121, 8719-8730 (2017)
The measurement of dipolar couplings among directly bonded nuclei yields direct information on the amplitude of dynamic processes in the solid-state. For a reliable motional analysis using, e.g., the model-free approach, a correct quantification of the absolute values of these order parameters is absolutely essential. In the absence of a reference value for the rigid limit, too low dipolar coupling values might be misinterpreted as motion. Therefore, a detailed understanding of the effects that influence the quantification of the experimental order parameters is necessary. We compare here REDOR and CPPI derived order parameters assessed in 1 H-detected experiments, and discuss the influence of remote protons and rf inhomogeneity on the extracted dipolar coupling constant for MAS rotation frequencies in the range 20-100 kHz. Experimental results are furthermore compared with the order parameter obtained from a molecular dynamics simulation. We find that fast magic-Angle spinning up to 100 kHz can yield artifact-free REDOR based 1 H, 15 N order parameters for perdeuterated and 100% amide back-exchanged proteins, and potentially even in uniformly protonated samples. We believe that awareness of systematic errors introduced by the measurement and in the analysis of order parameters will yield a better understanding of the dynamic properties of a protein derived from solid-state NMR observables.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Solid-state Nmr; Nuclear-magnetic-resonance; Angle-spinning Nmr; Atomic-resolution Structure; Protein Backbone Dynamics; Fully Protonated Proteins; Dipolar Couplings; Amyloid Fibrils; Perdeuterated Proteins; Conformational Flexibility
ISSN (print) / ISBN
1520-6106
e-ISSN
1520-5207
Journal
Journal of Physical Chemistry B
Quellenangaben
Volume: 121,
Issue: 37,
Pages: 8719-8730
Publisher
American Chemical Society (ACS)
Publishing Place
Washington
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)