Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 121, Issue 37, Pages 8719-8730Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b06812
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Funding
- Helmholtz-Gemeinschaft
- Deutsche Forschungsgemeinschaft (G-NMR) [Re1435, SFB-1035]
- Center for Integrated Protein Science Munich (CIPS-M)
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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 RED OR and CPPI derived order parameters assessed in H-1-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 H-1,N-15 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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