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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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Chemical Shift: Internal References and Solvent Effects01:17

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In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
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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...
803
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

992
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
992
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

1.4K
The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
1.4K
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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

1.3K
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...
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Updated: May 4, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Solid state NMR: The essential technology for helical membrane protein structural characterization.

Timothy A Cross1, Vindana Ekanayake2, Joana Paulino3

  • 1National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, USA; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, USA; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|January 14, 2014
PubMed
Summary
This summary is machine-generated.

Solid-state NMR spectroscopy now enables timely, high-resolution structural determination of native helical membrane proteins within lipid environments, overcoming previous challenges in sample preparation and non-native structures.

Keywords:
Helical membrane proteinsMagic angle spinning NMRMembrane influence on structureMembrane protein environmentMembrane protein structureOriented sample NMRPISEMASolid state NMRStructural validation

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Determining helical membrane protein structures using NMR spectroscopy has been historically challenging.
  • The cellular membrane environment significantly influences protein structure, with non-native structures often observed.
  • Previous methods struggled with sample preparation for both solution and solid-state NMR.

Purpose of the Study:

  • To overcome the challenges in structural determination of helical membrane proteins.
  • To demonstrate the utility of solid-state NMR for native membrane protein structure analysis.
  • To highlight recent advancements enabling timely structural characterization.

Main Methods:

  • Advancements in protein expression, purification, and reconstitution.
  • Development of sample preparation techniques for solid-state NMR.
  • Application of solid-state NMR on both oriented and magic angle spinning samples.

Main Results:

  • Solid-state NMR successfully produced native structures of helical membrane proteins in proteoliposomes and bilayers.
  • High-resolution structural characterization of functional states is achievable.
  • Detergent-free lipid environments are suitable for structural analysis.

Conclusions:

  • Solid-state NMR spectroscopy is a powerful tool for characterizing native helical membrane protein structures in their native lipid environments.
  • Recent methodological progress allows for timely and accurate structural determination.
  • This technique presents a significant opportunity for the NMR community to advance biomedical research.