Structural Monitoring Articles & Analysis: Older
5 articles found
The intrinsic fluorescence of a protein mainly originates from the aromatic amino acids in its structure, such as tryptophan, tyrosine, and phenylalanine, which emit fluorescence under ultraviolet light. When the protein structure changes, such as folding, unfolding, or binding to ligands, its intrinsic fluorescence changes accordingly. Therefore, by measuring ...
Additionally, recombinant protein drugs can be used in combination with small molecule drugs to provide additional or synergistic benefits.The intrinsic fluorescence of proteins mainly originates from the aromatic amino acids in their structure, such as tryptophan, tyrosine, and phenylalanine, which emit fluorescence under ultraviolet light. When the protein ...
Meanwhile, by comparing ultraviolet absorption spectra under different conditions, changes in the secondary and tertiary structure of proteins can be indirectly inferred, thereby monitoring the structural integrity of the drug. ...
Ultraviolet-Visible (UV-Vis) Spectroscopy(1) PrincipleUV-Vis spectroscopy utilizes the absorption characteristics of proteins in the ultraviolet region (especially around 280 nm) to monitor structural changes.(2) OperationMeasure the ultraviolet absorption spectrum of a collagen solution at different temperatures. ...
Here are three ways that mass detection is being adopted for monitoring large molecules. 1. Increase Certainty in Monitoring Peptide Maps and Peptide Modifications For companies developing biologics, a trend is for MS methods to be employed by labs further downstream in late stage development and manufacturing/QC to monitor CQAs and ensure ...