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Related Concept Videos

NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

2.8K
The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
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Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

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Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei...
3.0K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.3K
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...
1.3K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

10.6K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
10.6K
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

1.5K
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
1.5K
Other Nuclides: 31P, 19F, 15N NMR01:16

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

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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...
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Quantitative Protein Disorder Assessment Using NMR Chemical Shifts.

Jakob T Nielsen1,2, Frans A A Mulder3,4

  • 1Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus C, Denmark. jtn@inano.au.dk.

Methods in Molecular Biology (Clifton, N.J.)
|July 23, 2020
PubMed
Summary

Intrinsically disordered proteins (IDPs) are crucial for biological functions. A new metric, the Chemical shift Z-score for assessing Order/Disorder (CheZOD Z-score), quantifies protein order-disorder balance using NMR data.

Keywords:
CheZODChemical shiftData interpretationIDPIntrinsically disordered proteinsNMR spectroscopyPOTENCIProtein conformationSoftware

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Protein disorder is essential for biological functions.
  • Intrinsically disordered proteins (IDPs) exhibit diverse disorder characteristics.
  • Quantitative, position-specific characterization of IDPs is crucial for understanding their roles.

Purpose of the Study:

  • To introduce a novel metric for quantifying the local order-disorder balance in proteins.
  • To provide a method for the experimental characterization of intrinsically disordered proteins (IDPs).
  • To enable fast and easy calculation of protein order/disorder status.

Main Methods:

  • Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Calculating the Chemical shift Z-score for assessing Order/Disorder (CheZOD Z-score).
  • Comparing experimental NMR chemical shifts with computed random coil reference values.

Main Results:

  • The CheZOD Z-score provides a quantitative measure of local protein order and disorder.
  • The method allows for position-specific assessment of disorder.
  • CheZOD Z-scores can be rapidly computed using a Python tool or a web server.

Conclusions:

  • The CheZOD Z-score is a valuable tool for the quantitative analysis of protein disorder.
  • This metric aids in understanding the complexity and functional significance of intrinsically disordered proteins (IDPs).
  • Accessible computational tools facilitate the widespread application of this method in protein research.