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Related Concept Videos

Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
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...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

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...
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.
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

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

Two-Dimensional (2D) NMR: Overview

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.

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Related Experiment Video

Updated: Jul 3, 2026

MRM Microcoil Performance Calibration and Usage Demonstrated on Medicago truncatula Roots at 22 T
10:22

MRM Microcoil Performance Calibration and Usage Demonstrated on Medicago truncatula Roots at 22 T

Published on: January 16, 2021

Saturation transfer double-difference NMR spectroscopy using a dual solenoid microcoil difference probe.

Scott J Bergeron1, Ian D Henry, Robert E Santini

  • 1Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907, USA.

Magnetic Resonance in Chemistry : MRC
|July 11, 2008
PubMed
Summary

Saturation Transfer Double Difference NMR (STDD-NMR) with a microcoil probe simplifies ligand-biomolecule binding studies. This method automatically cancels non-binding ligands and protein signals, yielding a clear binding event detection.

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Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
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Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Related Experiment Videos

Last Updated: Jul 3, 2026

MRM Microcoil Performance Calibration and Usage Demonstrated on Medicago truncatula Roots at 22 T
10:22

MRM Microcoil Performance Calibration and Usage Demonstrated on Medicago truncatula Roots at 22 T

Published on: January 16, 2021

Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
11:44

Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes

Published on: November 12, 2016

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Investigating ligand-biomolecule interactions is crucial for drug discovery and understanding biological processes.
  • Traditional NMR methods for studying these interactions can be limited by concentration requirements and complex data analysis.
  • Saturation Transfer Double Difference Nuclear Magnetic Resonance (STDD-NMR) offers a promising alternative for sensitive detection of binding events.

Purpose of the Study:

  • To report the development and application of a novel solenoid microcoil NMR difference probe for collecting STDD-NMR spectra.
  • To demonstrate the probe's capability in automatically and internally canceling non-binding ligands and protein signals.
  • To evaluate the efficiency and effectiveness of this approach for studying ligand-biomolecule binding.

Main Methods:

  • Utilized a solenoid microcoil NMR difference probe designed for simultaneous sample signal acquisition and common signal cancellation.
  • Employed the STDD-NMR pulse sequence for spectral acquisition.
  • Applied the method to a system comprising human serum albumin (HSA) with octanoic acid (binding ligand) and glucose (non-binding ligand).

Main Results:

  • The NMR difference probe successfully and automatically subtracted the HSA protein signal.
  • Internal cancellation of the non-binding ligand (glucose) was achieved through phase cycling.
  • A clear proton NMR resonance signal from the binding ligand (octanoic acid) was observed in the final double difference spectrum.
  • The method provided good protein background subtraction and a clean signal for the binding ligand.

Conclusions:

  • The solenoid microcoil NMR difference probe combined with the STDD-NMR pulse sequence enables efficient and automated double difference experiments.
  • This integrated approach significantly simplifies the analysis of ligand-biomolecule binding, offering improved sensitivity and reduced background noise.
  • The developed method presents a favorable alternative to conventional approaches for investigating biomolecular interactions using NMR spectroscopy.