Site-specific dynamics of methyl groups probed by temporal evolution of heteronuclear 13C{1H} Overhauser polarisation encoded in 13C – 13C solid-state NMR correlation experiments

[Display omitted] •Methyl groups dynamics.•Biomolecules.•Pf1 bacteriophage virus•Solid-state NMR.•Heteronuclear Overhauser effect. There is great interest in studying the dynamics of methyl groups which are sensitive probes of local packing and molecular motions in biosolids and proteins. In this wo...

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Published in:Chemical physics letters 2020-09, Vol.754, p.137628, Article 137628
Main Authors: Purusottam, Rudra N., Tekely, Piotr
Format: Article
Language:English
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Summary:[Display omitted] •Methyl groups dynamics.•Biomolecules.•Pf1 bacteriophage virus•Solid-state NMR.•Heteronuclear Overhauser effect. There is great interest in studying the dynamics of methyl groups which are sensitive probes of local packing and molecular motions in biosolids and proteins. In this work we show that the magnetisation created by transient heteronuclear 13C{1H} Overhauser effect can be exploited in two-dimensional 13C – 13C solid-state NMR correlation experiments for straightforward access to site-specific dynamics of methyl groups in fully protonated 13C labelled biomolecules. The methodology developed for this purpose is demonstrated on polycrystalline L-isoleucine and applied to probe residue-specific dynamics of methyl groups in the coat protein of Pf1 bacteriophage filamentous virus.
ISSN:0009-2614
1873-4448
DOI:10.1016/j.cplett.2020.137628