Related Experiment Video
Updated: Dec 15, 2025

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Protein conformational changes affect the sodium triple-quantum MR signal.
Dennis Kleimaier1, Victor Schepkin2, Ruomin Hu1
1Computer Assisted Clinical Medicine, Heidelberg University, Mannheim, Germany.
Sodium triple-quantum (TQ) signals are sensitive to pH and protein unfolding. Changes in these factors significantly alter TQ signals, impacting their use as biomarkers in biological systems.
Area of Science:
- Biochemistry
- Biophysics
- Magnetic Resonance Imaging
Background:
- Sodium triple-quantum (TQ) signals are influenced by the local biochemical environment.
- Understanding these influences is crucial for interpreting in vivo sodium TQ MR signals.
Purpose of the Study:
- To investigate the dependence of sodium TQ signals on pH variations.
- To examine the impact of protein unfolding on sodium TQ signals.
- To assess the potential of sodium TQ signals as biomarkers in vivo.
Main Methods:
- Utilized a TQ time proportional phase increment pulse sequence to detect weak sodium TQ signals.
- Studied bovine serum albumin (BSA) over a pH range of 0.70 to 13.05.
- Induced protein unfolding using urea and monitored BSA structural changes via fluorescence microscopy.
Main Results:
- Minimum sodium TQ signal (1.34% ± 0.05%) observed at pH 0.70.
- Sodium TQ signal increased by 225% with pH elevation to 13.05.
- Urea-induced BSA unfolding increased sodium TQ signal by up to 40%.
Conclusions:
- Sodium TQ signal intensity correlates with the availability of negatively charged groups.
- Biochemical environment significantly affects sodium TQ MR signals.
- pH and protein unfolding are critical factors for interpreting in vivo sodium TQ signals as biomarkers of cell viability.
More Related Videos
09:25Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
14:55Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
¹H NMR: Interpreting Distorted and Overlapping Signals
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...
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
NMR Spectroscopy: Chemical Shift Overview
For instance, the proton...