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Cross polarization stability in multidimensional NMR spectroscopy of biological solids.

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Title: Cross polarization stability in multidimensional NMR spectroscopy of biological solids.
Authors: Harding, Benjamin D.1,2 (AUTHOR), Barclay, Alexander M.1,3 (AUTHOR), Piehl, Dennis W.4 (AUTHOR), Hiett, Ashley1,2 (AUTHOR), Warmuth, Owen A.1,2 (AUTHOR), Han, Ruixian5 (AUTHOR), Henzler-Wildman, Katherine2,6 (AUTHOR), Rienstra, Chad M.1,2,3,4,5,6,7,8 (AUTHOR) crienstra@wisc.edu
Source: Journal of Magnetic Resonance. Aug2024, Vol. 365, pN.PAG-N.PAG. 1p.
Subjects: Magic angle spinning, Nuclear magnetic resonance, Magnetic flux density, Quaternary structure, Tertiary structure
Abstract: [Display omitted] • Demonstration of temperature impact on cross polarization stability. • Use of thermopad attenuators to reduce the effect of temperature drift. • Influence of tangent ramp parameters on cross polarization efficiency and stability. • Application to microcrystalline, membrane, and fibrous proteins. Magic-angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) spectroscopy is a powerful and versatile technique for probing structure and dynamics in large, insoluble biological systems at atomic resolution. With many recent advances in instrumentation and polarization methods, technology development in SSNMR remains an active area of research and presents opportunities to further improve data collection, processing, and analysis of samples with low sensitivity and complex tertiary and quaternary structures. SSNMR spectra are often collected as multidimensional data, requiring stable experimental conditions to minimize signal fluctuations (t 1 noise). In this work, we examine the factors adversely affecting signal stability as well as strategies used to mitigate them, considering laboratory environmental requirements, configuration of amplifiers, and pulse sequence parameter selection. We show that Thermopad® temperature variable attenuators (TVAs) can partially compensate for the changes in amplifier output power as a function of temperature and thereby ameliorate one significant source of instability for some spectrometers and pulse sequences. We also consider the selection of tangent ramped cross polarization (CP) waveform shapes, to balance the requirements of sensitivity and instrumental stability. These findings collectively enable improved stability and overall performance for CP-based multidimensional spectra of microcrystalline, membrane, and fibrous proteins performed at multiple magnetic field strengths. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
Description
Abstract:[Display omitted] • Demonstration of temperature impact on cross polarization stability. • Use of thermopad attenuators to reduce the effect of temperature drift. • Influence of tangent ramp parameters on cross polarization efficiency and stability. • Application to microcrystalline, membrane, and fibrous proteins. Magic-angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) spectroscopy is a powerful and versatile technique for probing structure and dynamics in large, insoluble biological systems at atomic resolution. With many recent advances in instrumentation and polarization methods, technology development in SSNMR remains an active area of research and presents opportunities to further improve data collection, processing, and analysis of samples with low sensitivity and complex tertiary and quaternary structures. SSNMR spectra are often collected as multidimensional data, requiring stable experimental conditions to minimize signal fluctuations (t 1 noise). In this work, we examine the factors adversely affecting signal stability as well as strategies used to mitigate them, considering laboratory environmental requirements, configuration of amplifiers, and pulse sequence parameter selection. We show that Thermopad® temperature variable attenuators (TVAs) can partially compensate for the changes in amplifier output power as a function of temperature and thereby ameliorate one significant source of instability for some spectrometers and pulse sequences. We also consider the selection of tangent ramped cross polarization (CP) waveform shapes, to balance the requirements of sensitivity and instrumental stability. These findings collectively enable improved stability and overall performance for CP-based multidimensional spectra of microcrystalline, membrane, and fibrous proteins performed at multiple magnetic field strengths. [ABSTRACT FROM AUTHOR]
ISSN:10907807
DOI:10.1016/j.jmr.2024.107724