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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.6K
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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Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

7.5K
Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
7.5K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

1.5K
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...
1.5K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

1.6K
The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse....
1.6K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.5K
Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.5K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

743
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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Related Experiment Video

Updated: Mar 6, 2026

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
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Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

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Towards understanding cellular structure biology: In-cell NMR.

Safikur Rahman1, Younhwa Byun1, Md Imtaiyaz Hassan2

  • 1Department of Medical Biotechnology, Yeungnam University, Gyeongsan, 712-749, South Korea.

Biochimica Et Biophysica Acta. Proteins and Proteomics
|March 5, 2017
PubMed
Summary
This summary is machine-generated.

In-cell nuclear magnetic resonance (NMR) allows observing biomolecules within living cells at atomic resolution. This technique reveals crucial insights into protein structure, interactions, and dynamics in their native cellular environment.

Keywords:
In-cell NMRProtein maturationProtein stabilityProtein-protein interactionsStructure biologyα-Synuclein

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Area of Science:

  • Biophysics
  • Structural Biology
  • Cellular Biology

Background:

  • Observing biological macromolecules functioning within living cells is a long-standing goal in biology.
  • In-cell nuclear magnetic resonance (NMR) spectroscopy offers a powerful approach to study these molecules at the atomic level.

Purpose of the Study:

  • To review current methodologies in in-cell NMR.
  • To highlight its applications in understanding protein behavior within cells.

Main Methods:

  • In-cell NMR spectroscopy is employed to analyze biomolecular structures, interactions, and dynamics.
  • The technique is applicable across various cellular systems.

Main Results:

  • In-cell NMR provides atomic-level insights into protein interactions, folding, stability, and post-translational modifications.
  • It enables the study of intricate biological processes in their native cellular context.

Conclusions:

  • In-cell NMR is an effective tool for structural analysis and studying complex biological mechanisms within cellular environments.
  • This review underscores the value of in-cell NMR for advancing biological research.