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Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments

Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments
Resonance assignment is the first stage towards solving the structure of a protein. This is normally achieved by the employment of separate inter and intra residue experiments. By utilising the mixed rotation and rotary recoupling (MIRROR) condition it is possible to double the information content through the efficient bidirectional transfer of magnetization from the CO to its adjacent Ca and the Ca of the subsequent amino acid. We have incorporated this into a 3Dexperiment, a 3D-MIRROR NCOCA, where correlations present in the 3D spectrum permit the sequential assignment of the protein backbone from a single experiment as we have demonstrated on a microcrystalline preparation of GB3. Furthermore, the low power requirements of the MIRROR recoupling sequence facilitate the development of a low-power 3D-NCOCA experiment. This has enabled us to realise significant reductions in acquisition times, allowing the acquisition of a single 3D-NCOCA spectrum suitable for a full backbone resonance assignment of GB3 in less than 24 hours.
0925-2738
Jolly, M.M.
c927d250-88b0-4675-b8da-237cb0c0f0b1
Jarvis, J.A.
59de8efd-053f-49da-80b4-8df7b74fa325
Carravetta, M.
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Levitt, M.H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Jolly, M.M.
c927d250-88b0-4675-b8da-237cb0c0f0b1
Jarvis, J.A.
59de8efd-053f-49da-80b4-8df7b74fa325
Carravetta, M.
1b12fa96-4a6a-4689-ab3b-ccc68f1d7691
Levitt, M.H.
bcc5a80a-e5c5-4e0e-9a9a-249d036747c3
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a

Jolly, M.M., Jarvis, J.A., Carravetta, M., Levitt, M.H. and Williamson, P.T.F. (2017) Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments. Journal of Biomolecular NMR. (doi:10.1007/s10858-017-0147-0).

Record type: Article

Abstract

Resonance assignment is the first stage towards solving the structure of a protein. This is normally achieved by the employment of separate inter and intra residue experiments. By utilising the mixed rotation and rotary recoupling (MIRROR) condition it is possible to double the information content through the efficient bidirectional transfer of magnetization from the CO to its adjacent Ca and the Ca of the subsequent amino acid. We have incorporated this into a 3Dexperiment, a 3D-MIRROR NCOCA, where correlations present in the 3D spectrum permit the sequential assignment of the protein backbone from a single experiment as we have demonstrated on a microcrystalline preparation of GB3. Furthermore, the low power requirements of the MIRROR recoupling sequence facilitate the development of a low-power 3D-NCOCA experiment. This has enabled us to realise significant reductions in acquisition times, allowing the acquisition of a single 3D-NCOCA spectrum suitable for a full backbone resonance assignment of GB3 in less than 24 hours.

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More information

Accepted/In Press date: 21 October 2017
e-pub ahead of print date: 8 November 2017

Identifiers

Local EPrints ID: 415209
URI: http://eprints.soton.ac.uk/id/eprint/415209
ISSN: 0925-2738
PURE UUID: de6298ac-bb67-444d-82c0-d5a82cbe911d
ORCID for M. Carravetta: ORCID iD orcid.org/0000-0002-6296-2104
ORCID for M.H. Levitt: ORCID iD orcid.org/0000-0001-9878-1180
ORCID for P.T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

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Date deposited: 02 Nov 2017 17:30
Last modified: 18 Feb 2021 17:08

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