Andrea Soranno

Assistant Professor

Washington University in St. Louis

United States

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Andrea Soranno is an Assistant Professor at Washington University in St Louis, USA. His research focuses on biophysical mechanisms and the characterization of disordered proteins, as evidenced by his recent publications on the dynamics of the SARS-CoV-2 nucleocapsid protein and the interaction of RNA with intrinsically disordered regions. His work integrates experimental and computational techniques to explore the structural and functional aspects of proteins in cellular environments.

Articles (15)

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2025

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2020

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2020

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2020

Collaborators (6)

Gregory R. Bowman

Washington University School of Medicine

UNITED STATES

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Dennis Goldfarb

Assistant Professor

Washington University

UNITED STATES

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Erik Martin

UNITED STATES

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Alex Holehouse

Assistant Professor

Washington University in Saint Louis School of Medicine

UNITED STATES

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Michael Strickland

Washington University in St. Louis

UNITED STATES

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Peter Schuck

National Institutes of Health

UNITED STATES

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Andrea Soranno

Research Interests

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Articles (15)

The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer

Stabilization of interdomain closure by a G protein inhibitor

The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA

Accounting for Fast vs Slow Exchange in Single Molecule FRET Experiments Reveals Hidden Conformational States

Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations

Condensation Goes Viral: A Polymer Physics Perspective

Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail

The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins

Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein

The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy

Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective

A multi-step nucleation process determines the kinetics of prion-like domain phase separation

Valence and patterning of aromatic residues determine the phase behavior of prion-like domains

Apolipoprotein E: Structural Insights and Links to Alzheimer Disease Pathogenesis.

Depletion interactions modulate the binding between disordered proteins in crowded environments.

Collaborators (6)

Gregory R. Bowman

Dennis Goldfarb

Erik Martin

Alex Holehouse

Michael Strickland

Peter Schuck

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