01/27/21 The work led by Jasmine (in collaboration with Alex Holehouse and Greg Bowman) on the SARS CoV-2 nucleocapsid protein is featured on the NYT!

05/10/20 Jasmine and Jhullian have presented their new results on the SARS CoV-2 nucleocapsid protein at the 34th Annual Gibbs Conference for Thermodynamics.

09/21/20 Jasmine and Jhullian are the recipients of a MilliporeSigma fellowship. Congratulations!

06/18/20 A new preprint from our group and Alex Holehouse’s group exploring the biophysical behavior of SARS-CoV-2 nucleocapsid protein is now on Bioarxiv. Work led by Jasmine Cubuk together with Jhullian J. Alston, Jeremias Incicco, Sukrit Singh, Greg Bowman and others.

03/05/20 Andrea’s review on the “Physical basis of the disorder-order transition” is now published on Archives of Biochemistry and Biophysics.

02/17/20 Melissa presents her work on Apolipoprotein E at the Annual Meeting of Biophysical Society – Poster B004!

02/15/20 Andrea co-chairs the Intrinsically Disordered Protein subgroup at the Annual Meeting of Biophysical Society in San Diego.

02/07/20 “Valence and patterning of aromatic residues determine the phase behavior of prion-like domains”, a work with the groups of Tanjia Mittag (St Jude) and Rohit Pappu (WashU), is now out on Science. As a part of this work, we use FCS to measure concentrations and diffusion in the light and dense phase of phase-separated solutions. Congratulations to Jere and all the other authors!

02/04/20 Andrea presents the work on Apolipoprotein E at Duke. We are all very grateful for the support of the Ruth K. Broad Foundation to our research!

02/03/20 Rashmi and Debjit join the group! Welcome to our lab!

12/14/19  “Depletion interactions modulate coupled folding and binding in crowded environments”, a work with Franziska Zosel, Daniel Nettels, and Ben Schuler, is now out on Arxiv.

12/03/19 “The trap in the FRAP” is now out on Biophysical Journal.

11/19/19 “Branched unwinding mechanism of the Pif1 family of DNA helicases” is now out on PNAS.

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Our main research interests are the physical principles and molecular mechanisms determining biomolecular function. A particular focus are intrinsically disordered proteins (IDPs). At variance with the classical structure-function paradigm that we are familiar with from 50 years of structural biology, IDPs lack a persistent structure but, nevertheless, participate in many biological processes such as transcription, translation and signal transduction. In our lab, we combine fluorescence single-molecule spectroscopy with concepts from polymer physics to explain fundamental properties of disordered proteins, such as the role of electrostatic interactions, ion screening and macromolecular crowding on their conformations, as well as the contribution of internal friction to their dynamics. We are particularly interested in developing new tools to investigate the role of disordered proteins in intracellular phase transitions.

2020

• Zosel F, Soranno A, Nettels D, Schuler B. Depletion interactions modulate coupled folding and binding in crowded environments. arXiv preprint arXiv:1912.06783
• Martin EW, Holehouse AS, Peran I, Farag M,  Incicco JJ, Bremer A, Grace CR, Soranno A, Pappu RV, Mittag T. Valence and patterning of aromatic residues determine the phase behavior of prion-like domains. Science 367 (6478), 694-699

2019

• Soranno A. The Trap in the FRAP: A Cautionary Tale about Transport Measurements in Biomolecular Condensates. Biophys. J.
• Singh SP, Soranno A, Sparks MA, Galletto R. Branched unwinding mechanism of the Pif1 family of DNA helicases. Proc. Natl. Acad. Sci. USA.

2018

• Soranno A, Zosel F,Hofmann H. Internal friction in an intrinsically disordered protein—Comparing Rouse-like models with experiments. J. Chem. Phys.
• Soranno A, Cabassi F, Orselli ME, Cellmer T, Gori A, Longhi R, Buscaglia M Dynamics of Structural Elements of GB1 β-Hairpin Revealed by Tryptophan–Cysteine Contact Formation Experiments. J. Phys. Chem. B 122 (49), 11468-11477 
• Rezaei-Ghaleh N, Parigi G, Soranno A, Holla A, Becker S, Schuler B, Luchinat C, Zweckstetter M, Local and Global Dynamics in Intrinsically Disordered Synuclein, Angew.Chemie
• Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. Extreme disorder in an ultra-high-affinity protein complex, Nature

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In our lab we investigate disordered proteins at the interface between Biology, Chemistry, and Physics, combining state of the art single-molecule fluorescence spectroscopy and advanced theoretical models. In particular, we are interested in understanding the role of disordered regions in the formation of membraneless organelles  by investigating model systems in vitro and in living cells.

We are currently looking for:

• PostDocs: interested candidates should have a background in biophysics, protein biochemistry, cell biology, biomedical engineering, or a closely related field. Excellent verbal and written communication skills are required. Interested candidates should send a cover letter, C.V.,  a brief description of their past research accomplishments, and the contact information for three references to soranno@wustl.edu.
• Graduate students interested in working in our lab can contact Andrea Soranno directly, but should apply through one of the PhD programs (Biochemistry, Computational and Molecular Biophysics, etc…) at Washington University in Saint Louis.
• Undergraduate students interested in single-molecule spectroscopy and its application to intrinsically disordered proteins can contact Andrea Soranno directly.