Radiation damping in microcoil NMR probes

Krishnan, Viswanathan V

doi:10.1016/j.jmr.2005.12.011

Cited by 9 publications

(6 citation statements)

References 36 publications

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“…These strong samples have the added bonus that it is quite easy to see what the necessary wash out volume must be, and relaxation from radiation damping helps with our short relaxation delays [10]. Samples are injected into a fixed volume sample loop, then pushed into the probe with the HTSL pump.…”

Section: Methodsmentioning

confidence: 99%

Capillary scale NMR flow mapping

Massefski¹

2008

Journal of Magnetic Resonance

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Section: Methodsmentioning

confidence: 99%

Capillary scale NMR flow mapping

Massefski¹

2008

Journal of Magnetic Resonance

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“…Particular care for water-signal handling is needed in experiments conducted at high magnetic field strength (> 800 MHz, as 1 H Larmor frequency) or conducted with a highly-sensitive cryogenic probe [61–65]. An increase in the Q-factor, due to an increase in the magnetic field strength and/or by use of a “cold probe”, may result in significant radiation damping, even when the residual transverse water magnetization is small: a small residual of transverse magnetization induces a current in the coil, which in turn causes -Z-magnetization to return to +Z [66–68].…”

Section: Characteristics Of Protein Nmrmentioning

confidence: 99%

Protein-Inhibitor Interaction Studies Using NMR

Ishima

2015

Applications of NMR Spectroscopy

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Solution-state NMR has been widely applied to determine the three-dimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.

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“…A detailed investigation by Krishnan, however, suggests otherwise [78]. There are few differences between the standard NMR probes and microcoil NMR probes; most detectors with probe volumes greater than 50 μL described in the literature, are based on Helmholtz saddle coils [79,80].…”

Section: Measurement Of Radiation Dampingmentioning

confidence: 99%

“…The error bars determine the standard deviation over four consecutive measurements. (remade using the data presented in [78]. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.…”

Section: Figmentioning

confidence: 99%