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- W4211184178 endingPage "1651" @default.
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- W4211184178 abstract "Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial deuteration. This potentiates both the number of accessible target proteins and possibilities to exploit side-chain protons as reporters on distances and interactions. Their low dispersion, however, has severely compromised their chemical-shift assignment, which is a prerequisite for their use in downstream applications. Herein, we show that unambiguous correlations are obtained from 5D methodology by which the side-chain resonances are directly connected with the backbone. When further concatenated with simultaneous 4D intra-side-chain correlations, this yields comprehensive assignments in the side chains and hence allows a high density of distance restraints for high-resolution structure calculation from minimal amounts of protein." @default.
- W4211184178 created "2022-02-13" @default.
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- W4211184178 creator A5044683103 @default.
- W4211184178 creator A5065078318 @default.
- W4211184178 date "2022-02-11" @default.
- W4211184178 modified "2023-10-16" @default.
- W4211184178 title "Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment" @default.
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- W4211184178 doi "https://doi.org/10.1021/acs.jpclett.1c04075" @default.
- W4211184178 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35147439" @default.
- W4211184178 hasPublicationYear "2022" @default.
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