Related Experiment Video
Updated: Jan 27, 2026

Application and Methodology of the Non-destructive 19F Time-domain NMR Technique to Measure the Content in Fluorine-containing Drug Products
Published on: August 22, 2017
A nondestructive and noninvasive method to determine water content in lyophilized proteins using low-field
Anuji Abraham1, Omar Elkassabany1, Mary E Krause1
1Drug Product Science and Technology, Bristol-Myers Squibb, New Brunswick, New Jersey.
Abstract:
Determining the moisture content in lyophilized solids is a fundamental step towards predicting the quality and stability of lyophilized products, but conventional methods are time-consuming, invasive, and destructive. High levels of residual moisture in a lyophilized product can lead to cake collapse, product degradation, and reduced shelf life. The aim of this study was to develop a fast, noninvasive, nondestructive, and inexpensive method for determining the moisture content in a lyophilized monoclonal antibody (mAb) formulation using benchtop low-field time-domain nuclear magnetic resonance spectroscopy.
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Body Water Content and Fluid Compartments
Linear Approximation in Time Domain
For a simple pendulum with a mass evenly distributed along its length and the center of mass located at half the pendulum's length,...
Conservation of Protein Domains
Protein-Drug Binding: Determination Methods
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Time-Domain Interpretation of PD Control
Consider the example of control of motor torque. Initially, a positive...

