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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)

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...
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: 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...
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...
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:
IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration01:16

IR Spectroscopy: Hooke's Law Approximation of Molecular Vibration

A covalently bonded heteronuclear diatomic molecule can be modeled as two vibrating masses connected by a spring. The vibrational frequency of the bond can be expressed using an equation derived from Hooke's law, which describes how the force applied to stretch or compress a spring is proportional to the displacement of the spring. In this case, the atoms behave like masses, and the bond acts like a spring.
According to Hooke's law, the vibrational frequency is directly proportional to the...

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Updated: May 9, 2026

In situ FTIR Spectroscopy as a Tool for Investigation of Gas/Solid Interaction: Water-Enhanced CO2 Adsorption in UiO-66 Metal-Organic Framework
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Second harmonic correlation spectroscopy: a method for determining surface binding kinetics and thermodynamics.

Krystal L Sly1, Sze-Wing Mok, John C Conboy

  • 1Department of Chemistry, University of Utah, 315 South 1400 East RM. 2020, Salt Lake City, Utah 84112, USA.

Analytical Chemistry
|August 10, 2013
PubMed
Summary
This summary is machine-generated.

Second Harmonic Correlation Spectroscopy (SHCS) accurately measures molecular binding kinetics and thermodynamics at surfaces. This label-free method efficiently determines adsorption and desorption rates, offering an alternative to conventional isotherm studies.

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Published on: November 21, 2017

Area of Science:

  • Surface Science
  • Spectroscopy
  • Biophysics

Background:

  • Understanding molecular interactions at interfaces is crucial for various scientific fields.
  • Conventional methods for measuring binding kinetics can be time-consuming and require significant analyte amounts.

Purpose of the Study:

  • To implement and validate Second Harmonic Correlation Spectroscopy (SHCS) for determining adsorption and desorption kinetics.
  • To measure the binding kinetics and thermodynamics of (S)-(+)-1,1'-bi-2-napthol (SBN) intercalation into a lipid bilayer.
  • To compare SHCS results with conventional binding isotherm studies.

Main Methods:

  • Utilized Second Harmonic Correlation Spectroscopy (SHCS) by analyzing local fluctuations of the second harmonic (SH) signal.
  • Collected SH signal at steady-state equilibrium above saturation concentration over time.
  • Applied a correlation model for surface-bound molecules to fit the autocorrelated SH signal.

Main Results:

  • Determined adsorption rate of SBN to DOPC bilayer as 2.7 ± 0.2 × 10(3) s(-1) M(-1).
  • Measured desorption rate of SBN from DOPC bilayer as 9 ± 4 × 10(-4) s(-1).
  • Calculated equilibrium binding constant of 3.0 ± 1.3 × 10(6) M(-1), consistent with conventional methods.

Conclusions:

  • SHCS provides accurate, label-free kinetic and thermodynamic binding data.
  • SHCS allows simultaneous determination of adsorption and desorption rates in a single experiment.
  • This technique is particularly advantageous when time and analyte are limited.