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Related Concept Videos

Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

6.8K
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...
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Structures of Solids02:22

Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Metallic Solids02:37

Metallic Solids

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Metallic solids such as crystals of copper, aluminum, and iron are formed by metal atoms. The structure of metallic crystals is often described as a uniform distribution of atomic nuclei within a “sea” of delocalized electrons. The atoms within such a metallic solid are held together by a unique force known as metallic bonding that gives rise to many useful and varied bulk properties.
All metallic solids exhibit high thermal and electrical conductivity, metallic luster, and malleability....
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Resonance02:52

Resonance

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The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O bonds.
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Network Covalent Solids02:18

Network Covalent Solids

16.1K
Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
16.1K
Molecular and Ionic Solids02:54

Molecular and Ionic Solids

20.0K
Crystalline solids are divided into four types: molecular, ionic, metallic, and covalent network based on the type of constituent units and their interparticle interactions.
Molecular Solids
Molecular crystalline solids, such as ice, sucrose (table sugar), and iodine, are solids that are composed of neutral molecules as their constituent units. These molecules are held together by weak intermolecular forces such as London dispersion forces, dipole-dipole interactions, or hydrogen bonds, which...
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Updated: Jan 25, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins

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Solid-state MAS NMR resonance assignment methods for proteins.

Victoria A Higman1

  • 1Department of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TU, UK.

Progress in Nuclear Magnetic Resonance Spectroscopy
|May 4, 2019
PubMed
Summary
This summary is machine-generated.

Resonance assignment in solid-state MAS NMR is crucial for protein studies. This review covers carbon and proton detection methods, isotopic labeling, and software for efficient protein structure determination.

Keywords:
LabellingProteinResonance assignmentSolid-state MAS NMR

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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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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Protein structure and function studies heavily rely on resonance assignment via NMR.
  • Solid-state Magic Angle Spinning (MAS) NMR has evolved significantly over two decades with diverse pulse sequences and methods.
  • Traditional 2D and 3D carbon-13 (13C)-detected experiments are widely used for backbone and side-chain resonance assignment.

Purpose of the Study:

  • To review and consolidate various solid-state MAS NMR assignment methodologies.
  • To highlight advancements in both carbon-detected and proton-detected NMR assignment techniques.
  • To discuss the role of isotopic labeling and software in facilitating resonance assignment.

Main Methods:

  • Review of established 2D and 3D 13C-detected NMR experiments.
  • Exploration of emerging proton-detected triple-resonance experiments enabled by advanced hardware.
  • Discussion of isotopic labeling strategies (e.g., 13C, 15N) and their impact on assignment.
  • Overview of software tools for manual and automated resonance assignment.

Main Results:

  • Solid-state MAS NMR assignment methods have diversified, moving from traditional 13C-detection to advanced proton-detection techniques.
  • Proton detection, facilitated by higher magnetic fields and spinning frequencies, offers new avenues for triple-resonance experiments.
  • Isotopic labeling and specialized software are increasingly important for tackling challenging assignments.
  • A comprehensive understanding of these methods aids in structural and functional characterization of proteins.

Conclusions:

  • Solid-state MAS NMR assignment methods continue to advance, offering powerful tools for protein structure determination.
  • The integration of proton detection and sophisticated software enhances the efficiency and scope of resonance assignment.
  • Continued development in NMR hardware and methodologies will further accelerate insights into protein structure-function relationships.