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Related Concept Videos

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

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

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

2D NMR: Overview of Homonuclear Correlation Techniques

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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...
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Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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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....
1.4K
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

2.3K
In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the...
2.3K
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

1.8K
Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
1.8K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.4K
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...
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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SAR by 1D NMR.

Neal J Zondlo1

  • 1Department of Chemistry and Biochemistry , University of Delaware , Newark , Delaware 19716 , United States.

Journal of Medicinal Chemistry
|October 31, 2019
PubMed
Summary

Researchers reveal how to use 1D Nuclear Magnetic Resonance (NMR) spectroscopy to uncover molecular conformational signatures. This method aids in optimizing drug compounds and synthesizing macrocycles in medicinal chemistry.

Area of Science:

  • Organic Chemistry
  • Medicinal Chemistry
  • Spectroscopy

Background:

  • 1D NMR spectroscopy is crucial for identifying organic molecules.
  • Information on molecular conformation from 1D NMR is often underutilized.
  • Understanding solution-state conformation is key to drug discovery.

Purpose of the Study:

  • To demonstrate the utility of 1D NMR data in identifying molecular conformational signatures.
  • To apply these signatures in optimizing drug candidates and macrocycle synthesis.
  • To bridge the gap between routine NMR analysis and conformational insights.

Main Methods:

  • Utilizing chemical shifts, chemical shift dispersion, and coupling constants from 1D NMR spectra.
  • Correlating solution-state NMR data with protein target binding information.

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  • Analyzing case studies to validate the approach for medicinal chemistry optimization.

    • Main Results:

    • Identified specific conformational signatures of molecules in their bound state using 1D NMR.
    • Demonstrated successful application in optimizing medicinal chemistry compounds.
    • Showcased utility in the development of linkers for macrocycle synthesis.

    Conclusions:

    • Routine 1D NMR spectra contain valuable, often overlooked, conformational information.
    • This approach enhances the optimization of small molecules for drug development.
    • The method is particularly applicable to linker design in macrocyclic drug synthesis.