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Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
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2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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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...
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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
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¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

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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...
2.1K
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.9K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Protein structure determination by combining sparse NMR data with evolutionary couplings.

Yuefeng Tang1, Yuanpeng Janet Huang1, Thomas A Hopf2

  • 11] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.

Nature Methods
|June 30, 2015
PubMed
Summary
This summary is machine-generated.

Determining protein structure using NMR is hard for large proteins. A new hybrid method, EC-NMR, combines NMR data with evolutionary information to accurately determine structures for proteins up to 41 kDa.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for determining protein structure.
  • Accurate structure determination is challenging for larger proteins due to incomplete and ambiguous experimental data.
  • Evolutionary sequence information offers complementary structural constraints.

Purpose of the Study:

  • To develop and validate a hybrid approach combining NMR spectroscopy and evolutionary data for protein structure determination.
  • To address the limitations of traditional NMR methods for larger proteins.

Main Methods:

  • Developed a hybrid approach termed evolutionary coupling-NMR spectroscopy (EC-NMR).
  • Integrated sparse NMR data with evolutionary residue-residue coupling information.
  • Applied the EC-NMR method to determine structures of proteins in the 6-41 kDa size range.

Main Results:

  • Demonstrated accurate protein structure determination using the EC-NMR approach.
  • Successfully determined structures for multiple proteins within the tested size range.
  • Showcased the utility of combining sparse NMR data with evolutionary constraints.

Conclusions:

  • The EC-NMR method enhances the accuracy and feasibility of protein structure determination, especially for larger proteins.
  • This hybrid approach overcomes limitations of traditional NMR spectroscopy.
  • EC-NMR provides a valuable tool for structural biology research.