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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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.
The...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

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...
X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...

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Related Experiment Video

Updated: May 18, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

[Structural study on small molecules in biological solid samples by using solid state NMR].

Shigeru Matsuoka1

  • 1Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan. matsuokas11@chem.sci.osaka-u.ac.jp

Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan
|October 2, 2012
PubMed
Summary
This summary is machine-generated.

Solid-state NMR, specifically rotational-echo double-resonance (REDOR), enables atomic-level structural determination of insoluble biological molecules. This technique is crucial for understanding drug mechanisms and cellular processes without sample extraction.

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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Related Experiment Videos

Last Updated: May 18, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Area of Science:

  • Biophysics
  • Structural Biology
  • Analytical Chemistry

Context:

  • Many essential drug targets are insoluble biological matrices like membrane proteins.
  • Existing methods (solution NMR, X-ray crystallography) require solubilization or crystallization, often altering native structures.
  • Understanding atomic-level binding structures is key to elucidating drug action mechanisms.

Purpose:

  • To introduce rotational-echo double-resonance (REDOR) solid-state NMR as a technique for studying insoluble biological samples ('biological solids').
  • To demonstrate the application of REDOR NMR for high-resolution distance measurements in complex biological systems.
  • To showcase REDOR NMR's utility in structural studies of drug-target interactions and cellular metabolites.

Summary:

  • Rotational-echo double-resonance (REDOR) solid-state NMR provides indispensable high-resolution distance measurements for insoluble biological samples.
  • The paper details REDOR NMR applications, including structural analysis of the amphotericin B-membrane phospholipid complex.
  • It also highlights the structural elucidation of photorespiration metabolites in plant cells, achieved without prior extraction or isolation.

Impact:

  • Enables atomic-level structural determination of previously intractable biological targets, advancing drug discovery and development.
  • Provides insights into the function of membrane proteins and other insoluble biomolecules within their native-like environments.
  • Facilitates the study of complex cellular processes and metabolic pathways in situ, offering a deeper understanding of biological systems.