Single-molecule spectroscopy in living cells
Conformations of the disordered ensemble

NEWS

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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Research

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.

 

Publications

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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People

Andrea Soranno, PhD
Assistant Professor
soranno@wustl.edu

 

Melissa Brereton, PhD
Instructor
breretonm@wustl.edu

Jasmine Cubuk
PhD Candidate BBSB
cubukj@wustl.edu

Jhullian J Alston
PhD Candidate BBSB
alstonj@wustl.edu

co-mentored with Dr. Holehouse

J. Jeremias Incicco
Postdoc
inciccojj@wustl.edu

Debjit Roy
Postdoc
debjit.roy@wustl.edu

Rashmi Karki
Research Tech
karkir@wustl.edu

Owen Ouyang 
Undegraduate
wenhao.ouyang@wustl.edu

 

Logan Calderone
Undergraduate
lcalderone@wustl.edu

co-mentored by Dr. Brereton and Dr. Frieden

Former lab members

Marco Todisco 
visiting student,
PhD candidate in Physics, 
University of Milan (IT)

Pasquale Merolla 
Visiting Student,
MSc in Physics, U of Milan (IT),
now Thermo Fisher Scientific Italy

Open positions

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.

Contacts

Email

Dr. Andrea Soranno : soranno@wustl.edu

Phone

Office: (314) 273 16 32

Fax: (314) 362 71 83

Mail

Department of Biochemistry and Molecular Biophysics
660 St Euclid Ave, Campus Box 8231
Washington University in St. Louis
St. Louis, MO 63110


Dr. Soranno’s office is in room 2913 of the South Building of the School of Medicine. The lab is located in room 2908 and 2916 of the same building.