Greg Dignon @Dignon_Lab

Official account of Dignon lab at Rutgers Chemical and Biochemical Engineering. New Brunswick, NJ Joined September 2023

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Greg Dignon @Dignon_Lab

9 months ago

I'm excited for the new academic year and all that is in store, and very grateful to have such a great team to work with. Stay tuned for more publications coming out soon. If you are attending @ChEnected this November, look out for talks from myself and my lab members!

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Greg Dignon @Dignon_Lab

9 months ago

📝 I also submitted my first paper as sole corresponding author, with summer REU student Sophie Anderson and Rutgers undergrad Malcolm Harrison. Preprint: biorxiv.org/content/10.110…

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Greg Dignon @Dignon_Lab

9 months ago

Summer flew by! Amid some unexpected family health challenges, I’m proud of what my research group and I accomplished. Some highlights:

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Greg Dignon @Dignon_Lab

11 months ago

Finally sharing new work posted on biorxiv. We find that hydration free energy can serve as a quick and dirty approximation for globular protein partitioning into condensates. We also present a comparison of different hydration free energy methods. biorxiv.org/content/10.110…

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ShorterLab @ShorterLab

a year ago

Controlled and orthogonal partitioning of large particles into biomolecular condensates: nature.com/articles/s4146…

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Greg Dignon @Dignon_Lab

2 years ago

(17/17)I end with the TOC graphic which summarizes the approach to model "reactive" protein using a binding polynomial, the reduction of such protein's binding affinity, and the resulting reduction of its solution viscosity. Please reach out to me if you have questions/comments.

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Greg Dignon @Dignon_Lab

2 years ago

(16/17) Other modifications can be made to the procedure, but what is really necessary to have good confidence in any quantitative predictions would be more data. Future studies should leverage larger datasets to tune parameters involved in this procedure.

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Greg Dignon @Dignon_Lab

2 years ago

(1/17) Work from my postdoc at @LauferCenter finally out in @JCIM_JCTC ! Here we present an efficient procedure to evaluate the capability of small molecules to disrupt protein interactions, with a focus on drug formulations. See thread below: pubs.acs.org/doi/full/10.10…