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Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
Thermodynamic Potentials01:26

Thermodynamic Potentials

Thermodynamic potentials are state functions that are extremely useful in analyzing a thermodynamic system. They have dimensions of energy. The four important thermodynamic potentials are internal energy, enthalpy, Helmholtz free energy, and Gibbs free energy. These thermodynamic potentials can be expressed using two of the following variables: pressure, volume, temperature, and entropy. These two variables are expressed as the rate of change of the thermodynamic potential with respect to other...
Thermal Sigmatropic Reactions: Overview01:16

Thermal Sigmatropic Reactions: Overview

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Thermodynamic Systems

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Thermodynamics: Activity Coefficient

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Related Experiment Video

Updated: Jun 24, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Integrating Binding Thermodynamics and Relaxation for Evaluating Substrate-Dependent SABRE Performance.

Jingyi Wang1, Nan Zhuang1, Huijun Sun1

  • 1Department of Electronic Science, School of Electronic Science and Engineering, Fujian Provincial Key Laboratory of Plasma and Magnetic Resonance, Xiamen University, Xiamen 361005, P. R. China.

Analytical Chemistry
|June 22, 2026
PubMed
Summary

Substrate structure significantly impacts hyperpolarization efficiency in signal amplification by reversible exchange (SABRE). Stronger coordination to the iridium catalyst and slower relaxation enhance SABRE signal amplification.

Related Experiment Videos

Last Updated: Jun 24, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Area of Science:

  • Hyperpolarization techniques
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Catalysis

Background:

  • Signal amplification by reversible exchange (SABRE) is a parahydrogen-based hyperpolarization method offering high sensitivity.
  • Understanding the relationship between substrate structure and SABRE efficiency is crucial for optimization but remains poorly understood.

Purpose of the Study:

  • To investigate how substrate structure influences hyperpolarization efficiency in SABRE.
  • To elucidate the roles of coordination thermodynamics and relaxation dynamics in SABRE performance.

Main Methods:

  • Utilized 1H NMR, 2D diffusion-ordered spectroscopy (DOSY), and T1 relaxation measurements.
  • Probed coordination thermodynamics between pyridine/pyrazine derivatives and iridium catalyst precursors.
  • Analyzed substrate diffusion coefficients and spin-lattice relaxation times.

Main Results:

  • Higher SABRE signal enhancement correlated with larger coordination equilibrium constants (Keq) and decreased substrate self-diffusion upon ligation.
  • A direct correlation was observed between signal enhancement and Keq magnitude in a mixture of pyridine derivatives.
  • Rapid spin relaxation (shortened T1 values) of the substrate upon catalyst ligation negatively impacted hyperpolarization performance.

Conclusions:

  • Substrate coordination strength to the iridium catalyst precursor is a key factor determining SABRE hyperpolarization efficiency.
  • Relaxation dynamics play a significant role in retaining hyperpolarization, with faster relaxation leading to suboptimal performance.
  • These findings offer experimental insights into substrate-dependent SABRE performance, guiding future optimization strategies.