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Asami, S.* ; Reif, B.

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)
Verlagsversion DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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
Quellenangaben Band: 121, Heft: 37, Seiten: 8719-8730 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Verlagsort Washington
Begutachtungsstatus Peer reviewed