New paper in Biophys J! We used optical tweezers to show rhodium chrysi complexes both intercalate matched DNA AND insert into mismatches. One extra aromatic ring transforms the binding mode. Free access 50 days: authors.elsevier.com/a/1moAI1SPTF...

How does one protein do two jobs? Our new study shows how phosphorylation changes SARS-CoV-2 nucleocapsid from irreversibly compacting RNA (for packaging) to fast on/off binding (for replication). Part of a collaboration with the Musier-Forsyth lab at Ohio State. Link: doi.org/10.3390/v18010105

We measured single molecule ssDNA binding by SSB proteins from different systems, E. coli SSB, T4 gene 32, and LINE-1 ORF1p. All showed surprising initial compaction then decompaction. This allows them to dissociate rapidly in response to crowding, as we show in QRB Discovery doi.org/10.1017/qrd....

When B DNA is overstretched, it converts to melted DNA or S-DNA. Overstretching has been controversial because the transitions are similar for the two states. With the Westerlund and Wilhelmsson labs, we show in NAR the B-to-S transition is much faster than melting academic.oup.com/nar/article/...

Force-induced melting and S-DNA pathways for DNA overstretching exhibit distinct kinetics

Abstract. It is widely appreciated that double stranded DNA (dsDNA) is subjected to strong and dynamic mechanical forces in cells. Under increasing tension

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How does the ORF1p perform its multiple functions to facilitate LINE1 retrotransposition? And what enables its ability to also facilitate replication of other retrotransposons? Find out in our newly published paper in Nucleic Acids Research doi.org/10.1093/nar/...

L1-ORF1p nucleoprotein can rapidly assume distinct conformations and simultaneously bind more than one nucleic acid

Abstract. LINE-1 (L1) is a parasitic retrotransposable DNA element, active in primates for the last 80–120 Myr. L1 has generated nearly one-third of the hu

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