Optimal control derived sensitivity-enhanced CA-CO mixing sequences for MAS solid-state NMR - Applications in sequential protein backbone assignments

BLAHUT, Jan, Matthias J BRANDL, Riddhiman SARKAR, Bernd REIF and Zdenek TOS. Optimal control derived sensitivity-enhanced CA-CO mixing sequences for MAS solid-state NMR - Applications in sequential protein backbone assignments. JOURNAL OF MAGNETIC RESONANCE OPEN. AMSTERDAM: ELSEVIER, 2023, 16-17, Dec, p. 1-9. ISSN 2666-4410. Available from: https://dx.doi.org/10.1016/j.jmro.2023.100122.

Basic information

• Original name: Optimal control derived sensitivity-enhanced CA-CO mixing sequences for MAS solid-state NMR - Applications in sequential protein backbone assignments
• Authors: BLAHUT, Jan, Matthias J BRANDL, Riddhiman SARKAR, Bernd REIF and Zdenek TOS (guarantor).
• Edition: JOURNAL OF MAGNETIC RESONANCE OPEN, AMSTERDAM, ELSEVIER, 2023, 2666-4410.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10609 Biochemical research methods
• Country of publisher: Netherlands
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• RIV identification code: RIV/00216224:90242/23:00133764
• Doi: http://dx.doi.org/10.1016/j.jmro.2023.100122
• UT WoS: 001134051900001
• Keywords in English: FULLY PROTONATED PROTEINS; CROSS-POLARIZATION; SPECTROSCOPY; RESONANCE; DYNAMICS SIMULATION; NCO
• Tags: CF NMR, ne MU, rivok
• Tags: International impact, Reviewed

Abstract

We have recently introduced optimal-control derived pulse sequences for sensitivity-enhanced heteronuclear correlation NMR experiments of solid proteins. Preservation of equivalent coherence transfer pathways using transverse-mixing pulses (TROP) in multidimensional pulse schemes allows to increase the sensitivity of the experiments by more than a factor of root 2 per each indirect dimension. In this article, we present homonuclear CA-CO transverse-mixing elements (homoTROP) that are based on dipolar interactions and achieve similar gains as the heteronuclear TROP pulses described previously. Both transfer elements were subsequently implemented in 3D se-hCAcoNH and se-hCOcaNH, that together with the previously introduced 3D se-hCANH and se-hCONH experiments yield a complete set of sensitivity-enhanced protein backbone assignment experiments. In contrast to the J-coupling based methods that are used at fast (60 kHz) and ultrafast MAS (>100 kHz), the homoTROP experiments employ about 10-times shorter mixing times making use of the larger magnitude of the dipolar coupling in comparison to the J couplings. The experiments are demonstrated using a microcrystalline, perdeuterated sample of the chicken alpha-spectrin SH3 domain in which all exchangeable sites are fully back-substituted with protons. We evaluated the gains in efficiency in all experiments site-specifically observing that the se-hCAcoNH and se-hCOcaNH experiments yield an increase in sensitivity by a factor of 1.36 +/- 0.09 and at least a factor of 1.8 with respect to the conventional hcoCAcoNH and hCOcaNH J-based experiments.

Links

• 90242, large research infrastructures: Name: CIISB III