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Related Concept Videos

Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

873
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...
873
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.0K
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.
4.0K
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

930
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....
930
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

319
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...
319
Other Nuclides: 31P, 19F, 15N NMR01:16

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

481
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...
481
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.1K
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...
1.1K

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Updated: Oct 1, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Solid-State NMR: Methods for Biological Solids.

Sahil Ahlawat1, Kaustubh R Mote1, Nils-Alexander Lakomek2

  • 1Tata Institute of Fundamental Research Hyderabad, Survey No. 36/P Gopanpally, Serilingampally, Ranga Reddy District, Hyderabad 500046, Telangana, India.

Chemical Reviews
|March 3, 2022
PubMed
Summary
This summary is machine-generated.

Solid-state nuclear magnetic resonance (ssNMR) spectroscopy now deciphers complex biological structures and dynamics. Advances in hardware, methods, and sensitivity have made ssNMR a powerful tool for studying proteins and fibrils.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Solid-state nuclear magnetic resonance (ssNMR) has evolved from studying small molecules to analyzing complex biological systems.
  • Key advancements include hardware, sample preparation, pulsed methods, isotope labeling, resolution, and sensitivity improvements.
  • Unlike solution NMR, ssNMR accounts for the absence of molecular tumbling in solid samples.

Purpose of the Study:

  • To review state-of-the-art ssNMR methods for biological samples.
  • To discuss recent developments enhancing sensitivity and data acquisition speed.
  • To highlight ssNMR applications in solving protein structures and characterizing biological assemblies.

Main Methods:

  • Review of static and MAS (Magic Angle Spinning) pulsed NMR methods for biological samples.
  • Discussion of advanced signal filtering, proton methodologies, and multiple acquisition techniques.
  • Focus on methods applicable to biological systems with long rotational correlation times (>100 ns).

Main Results:

  • ssNMR is now a potent tool for determining the structure and dynamics of complex biological systems.
  • Examples of solved protein structures (globular, membrane, fibrils, assemblies) using ssNMR are presented.
  • Integrated approaches for characterizing challenging biological systems are discussed.

Conclusions:

  • ssNMR spectroscopy has been transformed into a powerful technique for structural biology.
  • Recent methodological advancements continue to expand the scope and capabilities of ssNMR.
  • Emerging subdisciplines within ssNMR spectroscopy are broadening its applications.