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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.8K
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.
3.8K
Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

266
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...
266
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

268
Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
268
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

751
When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
751
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

783
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....
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Related Experiment Video

Updated: Aug 16, 2025

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

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Solid-state NMR - a complementary technique for protein framework characterization.

Linda Cerofolini1,2, Kiefer O Ramberg3, Luis C Padilla1,4

  • 1Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, Sesto Fiorentino 50019, Italy. fragai@cerm.unifi.it.

Chemical Communications (Cambridge, England)
|December 22, 2022
PubMed
Summary
This summary is machine-generated.

Solid-state NMR analysis offers a new method for studying protein frameworks, which are biomaterials with medical uses. This technique can characterize frameworks with low crystallinity, complementing existing methods.

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Area of Science:

  • Biomaterials Science
  • Biophysics
  • Materials Chemistry

Background:

  • Protein frameworks represent an emerging class of biomaterials with significant medical and technological potential.
  • Current characterization of these frameworks primarily relies on X-ray diffraction or scattering techniques.
  • There is a need for complementary analytical strategies to fully understand protein framework properties.

Purpose of the Study:

  • To introduce and validate solid-state Nuclear Magnetic Resonance (NMR) as a complementary technique for characterizing protein frameworks.
  • To demonstrate the applicability of solid-state NMR to both microcrystalline protein-macrocycle frameworks and rehydrated freeze-dried protein samples.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
  • Analyses were performed on a microcrystalline protein-macrocycle framework.
  • The rehydrated freeze-dried protein was also analyzed using solid-state NMR.

Main Results:

  • Solid-state NMR successfully provided analytical data for the protein-macrocycle framework.
  • The technique was also effective for analyzing the rehydrated freeze-dried protein.
  • The study demonstrates the feasibility of using solid-state NMR for framework characterization.

Conclusions:

  • Solid-state NMR is a viable complementary method for studying protein frameworks.
  • This methodology shows promise for the characterization of protein frameworks, particularly those with low crystallinity.
  • The findings may expand the toolkit for analyzing novel biomaterials.