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Related Concept Videos

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a high...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Measuring protein reduction potentials using 15N HSQC NMR spectroscopy.

Samantha L Taylor1, Harriet Crawley-Snowdon, Jane L Wagstaff

  • 1School of Bioscience, University of Kent, Canterbury, Kent, CT2 7NJ, UK.

Chemical Communications (Cambridge, England)
|January 31, 2013
PubMed
Summary

Nuclear Magnetic Resonance (NMR) spectroscopy determined the reduction potentials of four redox proteins. ERp18 was confirmed as a potent oxidoreductase, matching or exceeding the strength of PDI a.

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Published on: December 12, 2013

Area of Science:

  • Biochemistry
  • Biophysical Chemistry
  • Spectroscopy

Background:

  • Redox proteins play crucial roles in cellular processes.
  • Understanding their reduction potentials is key to elucidating their function.
  • Glutathione is a key cellular redox buffer.

Purpose of the Study:

  • To measure the reduction potentials of four specific redox proteins.
  • To compare the reducing strength of ERp18 against known oxidoreductases like PDI a.

Main Methods:

  • Utilized Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Employed (15)N HSQC protein resonance analysis.
  • Performed titration experiments with mixtures of oxidized and reduced glutathione.

Main Results:

  • Reduction potentials were successfully measured for four redox proteins.
  • Results for PDI a, PDI ab, and DsbA were consistent with existing literature.
  • ERp18 demonstrated a reduction potential comparable to or greater than PDI a.

Conclusions:

  • ERp18 functions as a significant oxidoreductase.
  • The study provides quantitative data on the reducing power of ERp18.
  • NMR spectroscopy is a viable method for assessing redox protein potentials.