Single Molecule Biophysics Lab @Northeastern
Boston, MA
Joined February 2017
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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 @NAR_Open doi.org/10.1093/nar/gkae1141
Williams Lab retweeted
🚨 New PhD Program Alert! 🚨
Explore the intersection of physics, biology, and chemistry w/ Northeastern’s Biophysics PhD program. Flexible curriculum, cutting-edge research - shape your path in science
🗓 Priority Deadline: Jan 15
🔗 Apply now: cos.northeastern.edu/biophys…
In @VirusesMDPI, our single molecule measurements of basic residue mutants reveal that HIV-1 NC condenses dsDNA via a primarily electrostatic mechanism, which is needed to maintain viral core stability during reverse transcription. doi.org/10.3390/v16060872
Williams Lab retweeted
New research on #HIV infection — spearheaded by a professor at @Northeastern — could lead to better drugs to treat the virus.
Read more: bit.ly/4bi9Ghw
ALT Tweezers hold a sample.
ALT Mark Williams works in a lab.
ALT Mark Williams works in a lab.
Our new @ScienceAdvances paper with the Pathak lab at NCI is described in a story on @NUGlobalNews news.northeastern.edu/2024/0…
What triggers HIV-1 capsid uncoating? In @ScienceAdvances, with the Pathak lab at NCI, we show long dsDNA from reverse transcription is required for uncoating, likely due to mechanical pressure regulated by the nucleocapsid protein. science.org/doi/10.1126/scia…
What triggers HIV-1 capsid uncoating? In @ScienceAdvances, with the Pathak lab at NCI, we show long dsDNA from reverse transcription is required for uncoating, likely due to mechanical pressure regulated by the nucleocapsid protein. science.org/doi/10.1126/scia…
The T4 gp32 CTD recruits and stabilizes proteins within the model T4 replication complex. Does it serve other roles? Our new @JMolBiol paper shows that the CTD facilitates rapid removal of gp32 from ssDNA to ensure prompt genomic processing. doi.org/10.1016/j.jmb.2024.1…
Williams Lab retweeted
A cause for celebration. The grand opening ceremony of EXP brought dignitaries, university leaders, and community members together.
Read more: bit.ly/3Sq35LR
Can the sequence nonspecific single-stranded DNA binding protein E. coli SSB detect DNA damage? @WilliamsLabNEU and @BeuningLabNEU collaborated to show in @BiophysJ that the SSB binding conformation changes in response to DNA damage. doi.org/10.1016/j.bpj.2023.0…
How are T4 gene 32 (gp32) proteins rapidly removed from a stable filament during DNA replication? Our new @NAR_Open paper shows how gp32 can wind ssDNA in multiple conformations to facilitate rapid protein dissociation. doi.org/10.1093/nar/gkad595 #opticaltweezers #singlemolecule
Williams Lab retweeted
V. Adrian Parsegian, who made fundamental contributions to soft condensed matter, biological materials science and biophysics, passed away today.
Williams Lab retweeted
Jason starts his summer research at Northeastern. Good Luck Jason for a productive summer. Thank you @WilliamsLabNEU for the opportunity.
We are pleased to announce that the registration for the ‘12th International Retrovirology Symposium: Assembly, Maturation and Uncoating’ is now open!
ramm2023.utah.edu/
The conference will be held at Snowbird Utah from Sept 6th to 9th, 2023.
Part of a great collaboration with the laboratories of @LugerLab, Jim Maher, and Georges Mer!
Like other HMGB proteins, human FACT destabilizes nucleosomes to facilitate transcription. Why is the rest of this large protein needed? doi.org/10.1016/j.celrep.202… shows that the SSRP1 HMGB domain coordinates with the SPT16 domain to facilitate nucleosome reassembly after disruption
Like other HMGB proteins, human FACT destabilizes nucleosomes to facilitate transcription. Why is the rest of this large protein needed? doi.org/10.1016/j.celrep.202… shows that the SSRP1 HMGB domain coordinates with the SPT16 domain to facilitate nucleosome reassembly after disruption
The N protein of SARS-CoV-2, the virus responsible for COVID-19, is essential for viral replication, making it an attractive drug target. The N protein contains two primary structural domains. How do they coordinate to compact the viral genome? Find out in doi.org/10.1093/nar/gkac1179
