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Related Concept Videos

NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

1.5K
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...
1.5K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
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...
1.0K
¹H NMR Chemical Shift Equivalence: Enantiotopic and Diastereotopic Protons00:58

¹H NMR Chemical Shift Equivalence: Enantiotopic and Diastereotopic Protons

1.8K
Replacing each alpha-hydrogen in chloroethane by bromine (or a different functional group) yields a pair of enantiomers. Such protons are called prochiral or enantiotopic and are related by a mirror plane. Enantiotopic protons are chemically equivalent in an achiral environment. Because most proton NMR spectra are recorded using achiral solvents, enantiotopic hydrogens yield a single signal.
In chiral compounds such as 2-butanol, replacing the methylene hydrogens at C3 produces a pair of...
1.8K
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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

1.1K
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...
1.1K
¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons01:03

¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

2.4K
Protons in identical electronic environments within a molecule are chemically equivalent and have the same chemical shift. The replacement test is a useful tool to identify chemical equivalence and predict NMR spectra. A substituent replaces each of the protons being examined and the resulting molecules are compared. If the same molecule is obtained, the protons are equivalent or homotopic. Replacement of any hydrogens in ethane by chlorine yields chloroethane because all six protons are...
2.4K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

652
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...
652

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Optimal-Control-Based Cβ Chemical Shift Encoding for Efficient Signal Assignment of Solid Proteins.

Hajime Tamaki1, Yoh Matsuki1

  • 1Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.

The Journal of Physical Chemistry. B
|November 17, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a novel nuclear magnetic resonance (NMR) method for solid proteins. It enhances signal assignment by encoding Cβ chemical shifts onto Cα signals, reducing measurement time and improving sensitivity for protein structure determination.

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR spectroscopy is crucial for protein structural and dynamic analysis.
  • Site-specific signal assignment, particularly Cα and Cβ chemical shifts, is vital for identifying amino acid residues.
  • Conventional methods for Cβ chemical shift acquisition in solid proteins are limited by sensitivity drops due to long transverse evolution times.

Purpose of the Study:

  • To develop a new method for efficient Cβ chemical shift acquisition in solid-state NMR.
  • To overcome the sensitivity limitations associated with conventional Cβ chemical shift measurements.
  • To enable faster and more accurate signal assignment for solid proteins.

Main Methods:

  • Development of a novel Cβ-encoding method combining an optimal control-based spin manipulation pulse and a spin-state filter.
  • Encoding Cβ chemical shifts onto the intensities of scalar-coupled Cα signals.
  • Application of the method to microcrystalline protein GB1 for sequential signal assignment.

Main Results:

  • The new method reduces the required transverse evolution time to less than half of previous methods.
  • Total measurement time is shorter compared to explicit Cβ shift evolution.
  • Successful sequential signal assignment was demonstrated for microcrystalline protein GB1.

Conclusions:

  • The proposed Cβ-encoding nearest-neighbor NMR technique is applicable to solid proteins for the first time.
  • This method offers improved efficiency and sensitivity for protein signal assignment.
  • The approach holds promise for analyzing more complex protein systems.