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On the use of ³J-coupling NMR data to derive structural information on proteins.

ABSTRACT: Values of ³J-couplings as obtained from NMR experiments on proteins cannot easily be used to determine protein structure due to the difficulty of accounting for the high sensitivity of intermediate ³J-coupling values (4-8 Hz) to the averaging period that must cover the conformational variability of the torsional angle related to the ³J-coupling, and due to the difficulty of handling the multiple-valued character of the inverse Karplus relation between torsional angle and ³J-coupling. Both problems can be solved by using ³J-coupling time-averaging local-elevation restraining MD simulation. Application to the protein hen egg white lysozyme using 213 backbone and side-chain ³J-coupling restraints shows that a conformational ensemble compatible with the experimental data can be obtained using this technique, and that accounting for averaging and the ability of the algorithm to escape from local minima for the torsional angle induced by the Karplus relation, are essential for a comprehensive use of ³J-coupling data in protein structure determination.

SUBMITTER: Smith LJ

PROVIDER: S-EPMC7897194 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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On the use of 3J-coupling NMR data to derive structural information on proteins.

Smith Lorna J LJ van Gunsteren Wilfred F WF Stankiewicz Bartosz B Hansen Niels N

Journal of biomolecular NMR 20210125 1

Values of 3J-couplings as obtained from NMR experiments on proteins cannot easily be used to determine protein structure due to the difficulty of accounting for the high sensitivity of intermediate 3J-coupling values (4-8 Hz) to the averaging period that must cover the conformational variability of the torsional angle related to the 3J-coupling, and due to the difficulty of handling the multiple-valued character of the inverse Karplus relation between torsional a ...[more]

PMID: 33492494

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Project description:The spectroscopic study of oxygen, a vital element in materials, physical, and life sciences, is of tremendous fundamental and practical importance. 17O solid-state NMR (SSNMR) spectroscopy has evolved into an ideal site-specific characterization tool, furnishing valuable information on the local geometric and bonding environments about chemically distinct and, in some favorable cases, crystallographically inequivalent oxygen sites. However, 17O is a challenging nucleus to study via SSNMR, as it suffers from low sensitivity and resolution, owing to the quadrupolar interaction and low 17O natural abundance. Herein, we report a significant advance in 17O SSNMR spectroscopy. 17O isotopic enrichment and the use of an ultrahigh 35.2 T magnetic field have unlocked the identification of many inequivalent carboxylate oxygen sites in the as-made and activated phases of the metal-organic framework (MOF) α-Mg3(HCOO)6. The subtle 17O spectral differences between the as-made and activated phases yield detailed information about host-guest interactions, including insight into nonconventional O···H-C hydrogen bonding. Such weak interactions often play key roles in the applications of MOFs, such as gas adsorption and biomedicine, and are usually difficult to study via other characterization routes. The power of performing 17O SSNMR experiments at an ultrahigh magnetic field of 35.2 T for MOF characterization is further demonstrated by examining activation of the MIL-53(Al) MOF. The sensitivity and resolution enhanced at 35.2 T allows partially and fully activated MIL-53(Al) to be unambiguously distinguished and also permits several oxygen environments in the partially activated phase to be tentatively identified. This demonstration of the very high resolution of 17O SSNMR recorded at the highest magnetic field accessible to chemists to date illustrates how a broad variety of scientists can now study oxygen-containing materials and obtain previously inaccessible fine structural information.

Dataset Information

On the use of ³J-coupling NMR data to derive structural information on proteins.

Publications

On the use of <sup>3</sup>J-coupling NMR data to derive structural information on proteins.

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