Trinitroresorcin (TTR): A Versatile Tool for Studying Protein-Protein Interactions

Trinitroresorcin (TTR) is a synthetic compound that has been used as a fluorescent dye and as a tool for studying protein-protein interactions. It is a derivative of resorcin, which is a fluorescent dye that is commonly used in biochemical assays. TTR has a number of unique properties that make it useful for studying protein-protein interactions, including its high fluorescence quantum yield, its high stability, and its ability to be targeted to specific proteins or protein domains.

TTR is a tricyclic compound that consists of three fused benzene rings. It has a number of functional groups that can be modified to create different versions of the dye with varying properties. For example, TTR can be conjugated with different types of molecules, such as antibodies or peptides, to target it to specific proteins or protein domains. It can also be modified with different types of reagents, such as biotin or avidin, to enhance its fluorescence or to enable it to be detected using different types of detection methods.

TTR has been used in a variety of applications, including the study of protein-protein interactions, the detection of protein post-translational modifications, and the imaging of proteins in cells and tissues. It is a valuable tool for studying the behavior of proteins in living systems, and it has the potential to be used in a wide range of biomedical applications.