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Related Concept Videos

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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 slanted or...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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...
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
Proteomics01:33

Proteomics

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

2D NMR: Overview of Heteronuclear Correlation Techniques

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 axis.

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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

Solid-state NMR spectroscopy of protein complexes.

Shangjin Sun1, Yun Han, Sivakumar Paramasivam

  • 1Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA.

Methods in Molecular Biology (Clifton, N.J.)
|December 15, 2011
PubMed
Summary
This summary is machine-generated.

Solid-state NMR (SSNMR) spectroscopy enables the study of large, insoluble protein assemblies that are difficult to analyze with traditional methods. This technique offers new insights into the structure and dynamics of complex biological molecules.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Published on: September 17, 2017

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein-protein interactions are crucial for biological functions.
  • Large, insoluble, or non-crystalline protein assemblies pose challenges for conventional structural biology techniques like X-ray crystallography and solution NMR.
  • Solid-state NMR (SSNMR) spectroscopy is an emerging technique adept at overcoming these limitations.

Purpose of the Study:

  • To present general SSNMR methodologies for structural and dynamics analyses of protein complexes.
  • To showcase the application of SSNMR to challenging protein assemblies.
  • To provide protocols for sample preparation, data collection, and analysis in SSNMR studies.

Main Methods:

  • Magic angle spinning (MAS) SSNMR spectroscopy.
  • Application of SSNMR to thioredoxin reassemblies, HIV-1 capsid protein assemblies, and microtubule-associated protein assemblies.
  • Detailed protocols for sample preparation, pulse sequences, spectra collection, and data analysis.

Main Results:

  • Demonstrated the utility of SSNMR for studying large and complex protein assemblies.
  • Provided specific examples of structural and dynamics insights gained from SSNMR analysis of protein complexes.
  • Established SSNMR as a powerful tool for investigating biological macromolecules intractable to other methods.

Conclusions:

  • SSNMR spectroscopy is a versatile and powerful technique for the structural and dynamics characterization of protein assemblies.
  • The presented methodologies and protocols facilitate the application of SSNMR to a wide range of challenging biological systems.
  • SSNMR significantly expands the scope of structural biology for studying complex protein interactions and formations.