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App note: Characterizing protein-DNA interactions with mass photometry
Mass photometry is a label-free bioanalytical tool that can characterize protein-DNA interactions by directly measuring the relative abundance of proteins, nucleic acids and the complexes they form in solution. This application note shows how mass photometry can contribute to the study of DNA damage response by characterizing the interaction between the telomeric repeat-binding factor 2 (TRF2) protein and its telomeric DNA target.
Additional resources
WEBINAR: Elucidating the composition of CRISPR-Cas12f1 complexes using mass photometry
This webinar explores how the CRISPR-Cas12f1 effector complex recognizes and cleaves DNA. Mass photometry was used to measure the stoichiometry of two miniature Cas12f1 ribonucleoprotein complexes, AsCas12f1 and SpCas12f1 in vitro. The results indicate that the Cas protein forms a binary complex with guide RNA and remains bound when interacting with target DNA, forming a ternary complex. Overall, the results reveal the composition of a compact CRISPR-Cas system and its impact on target recognition and DNA cleavage mechanisms.
BLOG: Studying protein-DNA interactions with mass photometry
In this blog post, we present a recent study that used mass photometry to investigate protein-DNA interactions. We then speak with the paper’s first author, Ananya Acharya, who explains how she and her colleagues used mass photometry to answer unique scientific questions about DNA repair mechanisms and compares it to other techniques.