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Related Concept Videos

Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

17.9K
Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
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NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.1K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.1K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.3K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.3K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.1K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.1K
NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

3.3K
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...
3.3K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.2K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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Related Experiment Video

Updated: Jan 30, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Characterizing Protein Hydration Dynamics Using Solution NMR Spectroscopy.

Christine Jorge1, Bryan S Marques1, Kathleen G Valentine2

  • 1Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.

Methods in Enzymology
|January 15, 2019
PubMed
Summary
This summary is machine-generated.

This study details a method using reverse micelles to improve protein hydration studies via Nuclear Overhauser Effect (NOE) and Rotating frame Overhauser Effect (ROE) spectroscopy. This technique overcomes limitations of bulk water and hydrogen exchange, enabling clearer insights into protein dynamics.

Keywords:
Hydration dynamicsHydrogen exchangeNuclear Overhauser effectProtein hydrationRelayed Overhauser effectRotating frame Overhauser effect

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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
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In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Protein hydration is crucial for stability, folding, and function, but experimentally challenging to study.
  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy, using Nuclear Overhauser Effects (NOE) and Rotating frame Overhauser Effects (ROE), offers site-resolved insights into protein-water interactions.
  • Traditional NMR methods face limitations like bulk water contamination and hydrogen exchange-relayed magnetization artifacts.

Purpose of the Study:

  • To present guidelines for preparing protein solutions encapsulated in reverse micelles for enhanced NOE and ROE spectroscopy.
  • To address and overcome experimental limitations in characterizing protein hydration dynamics.
  • To improve the accuracy and reliability of NMR-based studies on protein-water interactions.

Main Methods:

  • Encapsulation of single protein molecules within the water core of reverse micelles.
  • Utilizing NOE and ROE spectroscopy for characterizing protein-water interactions.
  • Detailed analysis of NOE intensity contributions, including those from hydrogen exchange-relayed magnetization.
  • Fitting of NOE, selectively decoupled NOE, and ROE time courses.

Main Results:

  • Reverse micelle encapsulation effectively suppresses hydrogen exchange and eliminates bulk water interference.
  • This method provides a cleaner signal for NOE and ROE measurements.
  • Guidelines are provided for preparing suitable solutions and analyzing spectral data.
  • Understanding and accounting for hydrogen exchange-relayed NOE is demonstrated.

Conclusions:

  • Reverse micelle encapsulation is a powerful strategy to overcome limitations in studying protein hydration dynamics using NMR.
  • This approach significantly enhances the site-resolved characterization of protein-water interactions.
  • The detailed guidelines facilitate the application of NOE and ROE spectroscopy for a deeper understanding of protein stability, folding, and function.