09/2026 Great news for our ApoE research! The NIH/NIA U19 program “Biology and Pathobiology of APOE in Aging and Alzheimer’s Disease 2.0” has been renewed. Andrea leads Project 1, focused on deciphering the structural and biochemical properties of APOE. We are excited to continue this work!

05/22/26 A new review from Drake, Jasmine, Nirnay, Melissa, and Andrea, “Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions”, is now out in Current Opinion in Structural Biology!

01/06/26 Our collaboration with Tommaso Bellini and colleagues on “Polymer conformational entropy as the driver of complex coacervation” is now out in PNAS. Congratulations to Tommaso Inzani and all the authors!

12/05/25 Congratulations to Nirnay for receiving the 2025 BMB Research Staff Scientist Excellence Award!

12/04/25 Our collaborative work on “Multiscale structure of chromatin condensates explains phase separation and material properties” is now published in Science! Congratulations to Nirnay and the entire collaborative team.

12/03/25 Congratulations to Klaudio for receiving the 2025 Elliot L. Elson Education and Training Award!

08/26/25 Our collaborative work on “Phosphorylation toggles the SARS-CoV-2 nucleocapsid protein between two membrane-associated condensate states” is now out in Nature Communications. Congratulations to Jasmine and all our collaborators!

07/16/25 Jasmine’s work on the SARS-CoV-2 nucleocapsid protein, “The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer”, is now published in Cell Reports Physical Science. Congratulations to Jasmine, Jere, Melissa, and our collaborators!

06/2025 We are excited to receive a new four-year NIH/NHLBI grant with Michael Greenberg and Alex Holehouse to study how sequence changes in intrinsically disordered regions of cardiac troponin alter its structural dynamics and function!

01/27/25 Andrea received a 2025 Dean’s Impact Award, recognizing enduring commitment and achievement in community engagement. Thank you to everyone in the lab and our community who makes mentoring and outreach possible!

01/20/25 Congratulations to Madison for being selected for the 2024 MilliporeSigma Predoctoral Fellowship!

09/03/24 Our collaborative study with the Blumer and Bowman groups, “Stabilization of interdomain closure by a G protein inhibitor”, is now out in PNAS. Congratulations to Tyson and all the authors!

06/13/24 Congratulations to Jasmine for receiving the 2024 W.M. Keck Postdoctoral Fellowship!

06/04/24 Congratulations to Jasmine for receiving the 2023 Ceil M. DeGutis Prize Fellows Award!

04/10/24 Congratulations to Andrea and Natalie Niemi for receiving the DBBS Outstanding Mentor Award. The award recognizes faculty who demonstrate exceptional mentorship, guidance, and support for graduate students.

04/01/24 Congratulations to Madison for receiving the 2024 Elliot L. Elson Education and Training Award!

03/21/24 Jasmine, Jhullian, Jere, Melissa and collaborators’ work, “The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA”, is now published in Nucleic Acids Research!

05/12/23 Congratulations to Madison for receiving the 2023 BMB Science Communication Award!

04/21/23 Congratulations to Jasmine for successfully defending her PhD thesis! We are very proud of everything she has accomplished in the lab.

02/07/23 Melissa’s work on the structural ensemble of Apolipoprotein E4, “Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms”, is now out in PNAS. Congratulations to Melissa, Upasana, Jere, Debjit, Jasmine, and all our collaborators!

01/08/23 Congratulations to Jasmine for being selected for the 2022 John E. Majors Fellowship Award!

04/2022 We are excited to receive a new five-year NIH/NIAID R01 with Kathleen Hall and Alex Holehouse for “A multipronged investigation of SARS-CoV-2 genome packaging”!

10/19/21 Congratulations to Jasmine for receiving the Elliot L. Elson Education and Training Award!

08/2021 We are excited to be part of a new NIH/NIA U19 program on the biology and pathobiology of ApoE in aging and Alzheimer’s disease. Our project will investigate the structure and biophysical properties of ApoE.

07/23/21 Our collaborative work with the Mittag lab, “A multi-step nucleation process determines the kinetics of prion-like domain phase separation”, is now out in Nature Communications!

03/29/21 Jasmine, Jhullian, Jere and collaborators’ work, “The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA”, is now published in Nature Communications. Congratulations to Jasmine and the entire team!

01/27/21 Jasmine and our work on the SARS-CoV-2 nucleocapsid protein are featured in the New York Times article “If You Squeeze the Coronavirus, Does It Shatter?” Jasmine discusses how single-molecule FRET can reveal the flexibility of the nucleocapsid protein and how its interactions with RNA may help package the viral genome. Congratulations Jasmine!

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

09/08/20 Congratulations to Jhullian for being selected for the 2020 MilliporeSigma Predoctoral Fellowship!

09/03/20 Congratulations to Jasmine for being selected for the 2020 MilliporeSigma Predoctoral Fellowship!

06/18/20 A new preprint from our group and the Holehouse group exploring the biophysical behavior of the SARS-CoV-2 nucleocapsid protein is now on bioRxiv. The work is led by Jasmine Cubuk together with Jhullian J. Alston, J. Jeremías Incicco, Sukrit Singh, Melissa Stuchell-Brereton, Greg Bowman, Kathleen Hall, Alex Holehouse, and collaborators.

06/02/20 “Depletion interactions modulate the binding between disordered proteins in crowded environments”, a collaborative work with Franziska Zosel, Karin Buholzer, Daniel Nettels, and Ben Schuler, is now out in PNAS!

03/13/20 A spotlight on the Soranno Lab, written by Marissa Locke, highlights our work on ApoE4 conformations and Alzheimer’s disease.

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

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

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

02/07/20 “Valence and patterning of aromatic residues determine the phase behavior of prion-like domains”, a collaboration with the groups of Tanja Mittag at St. Jude and Rohit Pappu at WashU, is now out in Science! As part of this work, we use fluorescence correlation spectroscopy to measure concentrations and diffusion in the dilute and dense phases of phase-separated solutions. Congratulations to Jere and all the authors!

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

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

12/03/19 “The Trap in the FRAP: A Cautionary Tale about Transport Measurements in Biomolecular Condensates” is now out in Biophysical Journal.

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

Our research focuses on the physical principles and molecular mechanisms that determine biomolecular function. A central theme of the lab is understanding intrinsically disordered proteins and regions (IDPs/IDRs). Unlike folded proteins, IDPs do not adopt a single persistent three-dimensional structure. Instead, they populate dynamic ensembles of conformations that enable them to participate in essential biological processes including transcription, RNA binding, signaling, molecular recognition, and biomolecular condensation.

We combine single-molecule fluorescence spectroscopy, ensemble biochemistry, and concepts from polymer and statistical physics to connect molecular-scale conformations and dynamics with biological function. Our work investigates how sequence, electrostatic interactions, ion screening, macromolecular crowding, molecular interactions, and internal friction shape the conformational behavior of disordered proteins.

A particular interest of the lab is understanding how the physical properties of disordered proteins regulate biomolecular condensates and phase transitions. We develop and apply quantitative single-molecule approaches to determine how proteins and nucleic acids interact in complex and crowded environments, and how these interactions give rise to biological function or dysfunction.

Current Research Directions

Intrinsically Disordered Proteins and Biomolecular Condensates

A major goal of the lab is to understand how the amino-acid sequence of an intrinsically disordered protein encodes its conformational ensemble, molecular interactions, and function. We use single-molecule spectroscopy to directly observe these heterogeneous and rapidly fluctuating molecules and combine these measurements with polymer-physics models and computational approaches.

We are especially interested in how weak multivalent interactions involving proteins and nucleic acids generate biomolecular condensates. By connecting the behavior of individual molecules with the collective properties of condensates, we aim to establish quantitative physical principles for biological phase separation.

Apolipoprotein E and Alzheimer’s Disease

Apolipoprotein E (APOE) is the strongest genetic modifier of risk for late-onset Alzheimer’s disease. APOE is highly dynamic, and its structural properties change upon oligomerization, lipid binding, and interaction with other biomolecules.

We use single-molecule fluorescence, biochemical approaches, structural methods, and molecular simulations to determine how different APOE variants alter protein conformations, interactions, and function. A major current focus is understanding the molecular mechanisms underlying APOE variants.

This work is part of the NIH/NIA program Biology and Pathobiology of APOE in Aging and Alzheimer’s Disease 2.0, in which the Soranno Lab leads Project 1.

Viral Nucleocapsid Proteins and Genome Packaging

Viral nucleocapsid proteins provide a powerful example of how structural disorder, RNA binding, and biomolecular condensation work together to produce biological function.

Our studies of the SARS-CoV-2 nucleocapsid protein have revealed how its intrinsically disordered regions regulate RNA interactions, dimerization, conformational dynamics, and phase separation. We combine single-molecule fluorescence, biochemical measurements, and computational approaches to understand how these molecular properties contribute to viral genome packaging.

More broadly, we are interested in determining how the physical principles encoded by disordered viral proteins are conserved across viruses and how changes in sequence alter their molecular behavior.

Disordered Regions in Cardiac Troponin

Intrinsically disordered regions are also central to the regulation of muscle contraction. In collaboration with the Greenberg and Holehouse laboratories, we investigate the structural dynamics of disordered regions within cardiac troponin.

Our goal is to understand how changes in protein sequence, including disease-associated mutations, reshape the conformational ensemble and molecular interactions of troponin and ultimately alter cardiac function. This project combines single-molecule measurements, molecular biophysics, and computational modeling to connect sequence-level changes with mechanisms of cardiovascular disease.

Our Approach

The lab develops and applies quantitative approaches including:

• Single-molecule Förster resonance energy transfer (smFRET)
• Fluorescence correlation spectroscopy (FCS)
• Single-molecule measurements of conformational dynamics and molecular interactions
• Biochemical and biophysical characterization of proteins and nucleic acids
• Polymer-physics and statistical-mechanical models of disordered proteins
• Studies of biomolecular condensation and phase separation
• Integration of experiments with molecular simulations and structural approaches through collaborative research

Together, these approaches allow us to investigate biological systems across scales—from the conformational fluctuations of individual molecules to the collective behavior of multicomponent biomolecular assemblies.

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2026

• Jensen D, Cubuk J, Samanta N, Stuchell-Brereton MD, Soranno A. Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions. Curr. Opin. Struct. Biol. 98, 103277 (2026)
• Phillips M, Holla A, Wojtas M, Chowdhury A, Sottini A, König SLB, Mutter N, Lamb N, Huihui J, Lopko M, Soranno A, Nettels D, Ożyhar A, Schuler B, Ghosh K. Mapping Charge Interactions in Intrinsically Disordered Proteins. Adv. Sci. 13 (16), e14056 (2026)
• Inzani T, Nava G, Buscaglia M, Soranno A, Gori A, Bergamaschi G, Suweis S, Maritan A, Bellini T. Polymer conformational entropy as the driver of complex coacervation. Proc. Natl. Acad. Sci. USA 123 (1), e2520181123 (2026)

2025

• Zhou H, Huertas J, Maristany MJ, Russell K, Hwang JH, Yao RW, Samanta N, Hutchings J, Billur R, Shiozaki M, Zhao X, Doolittle LK, Gibson BA, Soranno A, Riggi M, Espinosa JR, Yu Z, Villa E, Collepardo-Guevara R, Rosen MK. Multiscale structure of chromatin condensates explains phase separation and material properties. Science 390 (6777), eadv6588 (2025)
• Favetta B, Wang H, Cubuk J, Singh A, Barai M, Ramirez C, Zheng H, Gormley AJ, Murthy NS, Dignon G, Soranno A, Shi Z, Schuster BS. Phosphorylation toggles the SARS-CoV-2 nucleocapsid protein between two membrane-associated condensate states. Nat. Commun. 16, 7970 (2025)
• Cubuk J, Incicco JJ, Hall KB, Holehouse AS, Stuchell-Brereton MD, Soranno A. The dimerization domain of SARS-CoV-2 nucleocapsid protein is partially disordered and forms a dynamic high-affinity dimer. Cell Rep. Phys. Sci. 6 (7), 102695 (2025)

2024

• Miller JJ, Mallimadugula UL, Zimmerman MI, Stuchell-Brereton MD, Soranno A, Bowman GR. Accounting for Fast vs Slow Exchange in Single Molecule FRET Experiments Reveals Hidden Conformational States. J. Chem. Theory Comput. 20 (23), 10339-10349 (2024)
• Holla A, Martin EW, Dannenhoffer-Lafage T, Ruff KM, König SLB, Nüesch MF, Chowdhury A, Louis JM, Soranno A, Nettels D, Pappu RV, Best RB, Mittag T, Schuler B. Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations. JACS Au 4 (12), 4729-4743 (2024)
• Todd TD, Vithani N, Singh S, Bowman GR, Blumer KJ, Soranno A. Stabilization of interdomain closure by a G protein inhibitor. Proc. Natl. Acad. Sci. USA 121 (36), e2311711121 (2024)
• Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. Nucleic Acids Res. 52 (5), 2609-2624 (2024)
• Cubuk J, Greenberg L, Greenberg AE, Emenecker RJ, Stuchell-Brereton MD, Holehouse AS, Soranno A, Greenberg MJ. Structural dynamics of the intrinsically disordered linker region of cardiac troponin T. bioRxiv preprint 2024.05.30.596451 (2024)

2023

• Stringer MA, Cubuk J, Incicco JJ, Roy D, Hall K, Stuchell-Brereton MD, Soranno A. Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail. J. Phys. Chem. B 127 (26), 5837-5849 (2023)
• Stuchell-Brereton MD, Zimmerman MI, Miller JJ, Mallimadugula UL, Incicco JJ, Roy D, Smith LG, Cubuk J, Baban B, DeKoster GT, Frieden C, Bowman GR, Soranno A. Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. Proc. Natl. Acad. Sci. USA 120 (7), e2215371120 (2023)
• Alston JJ, Ginell GM, Soranno A, Holehouse AS. The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins. J. Phys. Chem. B 127 (21), 4746-4760 (2023)
• Mooren OL, Stuchell-Brereton MD, McConnell P, Yan C, Wilkerson EM, Goldfarb D, Cooper JA, Sept D, Soranno A. Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein. J. Mol. Biol. 435 (24), 168342 (2023)
• Alston JJ, Soranno A. Condensation Goes Viral: A Polymer Physics Perspective. J. Mol. Biol. 435 (16), 167988 (2023)
• Alston JJ, Soranno A, Holehouse AS. Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation. bioRxiv preprint 2023.08.06.552128 (2023)

2022

• Soranno A, Incicco JJ, De Bona P, Tomko EJ, Galburt EA, Holehouse AS, Galletto R. Shelterin Components Modulate Nucleic Acids Condensation and Phase Separation in the Context of Telomeric DNA. J. Mol. Biol. 434 (16), 167685 (2022)
• Cubuk J, Stuchell-Brereton MD, Soranno A. The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy. Essays Biochem. 66 (7), 875-890 (2022)
• Cubuk J, Soranno A. Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective. ChemSystemsChem 4, e202100051 (2022)
• Incicco JJ, Roy D, Stuchell-Brereton MD, Soranno A. Fluorescence Correlation Spectroscopy and Phase Separation. Methods Mol. Biol. 2563, 161-198 (2022)

2021

• Martin EW, Harmon TS, Hopkins JB, Chakravarthy S, Incicco JJ, Schuck P, Soranno A, Mittag T. A multi-step nucleation process determines the kinetics of prion-like domain phase separation. Nat. Commun. 12, 4513 (2021)
• Benke S, Holla A, Wunderlich B, Soranno A, Nettels D, Schuler B. Combining Rapid Microfluidic Mixing and Three-Color Single-Molecule FRET for Probing the Kinetics of Protein Conformational Changes. J. Phys. Chem. B 125 (24), 6617-6628 (2021)
• König I, Soranno A, Nettels D, Schuler B. Impact of In-Cell and In-Vitro Crowding on the Conformations and Dynamics of an Intrinsically Disordered Protein. Angew. Chem. Int. Ed. 60 (19), 10724-10729 (2021)
• Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Nat. Commun. 12, 1936 (2021)
• Alston JJ, Soranno A, Holehouse AS. Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins. Methods 193, 116-135 (2021)
• Chen Y, Strickland MR, Soranno A, Holtzman DM. Apolipoprotein E: Structural Insights and Links to Alzheimer Disease Pathogenesis. Neuron 109 (2), 205-221 (2021)

2020

• 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 (2020)
• Zosel F, Soranno A, Buholzer KJ, Nettels D, Schuler B. Depletion interactions modulate the binding between disordered proteins in crowded environments. Proc. Natl. Acad. Sci. USA 117 (24), 13480-13489 (2020)
• Soranno A. Physical basis of the disorder-order transition. Arch. Biochem. Biophys. 685, 108305 (2020)

2019

• Singh SP, Soranno A, Sparks MA, Galletto R. Branched unwinding mechanism of the Pif1 family of DNA helicases. Proc. Natl. Acad. Sci. USA 116 (49), 24533-24541 (2019)
• Soranno A. The Trap in the FRAP: A Cautionary Tale about Transport Measurements in Biomolecular Condensates. Biophys. J. 117 (11), 2041-2042 (2019)

2018

• 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 (2018)
• 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. Chem. Int. Ed. 57 (46), 15262-15266 (2018)
• Best RB, Zheng W, Borgia A, Buholzer K, Borgia MB, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Schuler B. Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”. Science 361 (6405), eaar7101 (2018)
• Soranno A, Zosel F, Hofmann H. Internal friction in an intrinsically disordered protein—Comparing Rouse-like models with experiments. J. Chem. Phys. 148 (12), 123326 (2018)
• 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 555, 61-66 (2018)

2017

• Soranno A, Holla A, Dingfelder F, Nettels D, Makarov DE, Schuler B. Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations. Proc. Natl. Acad. Sci. USA 114 (10), E1833-E1839 (2017)
• Zosel F, Haenni D, Soranno A, Nettels D, Schuler B. Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein. J. Chem. Phys. 147 (15), 152708 (2017)

Andrea’s publications prior to starting the Soranno Lab (2009–2016)

2016

• Borgia A, Zheng W, Buholzer K, Borgia MB, Schüler A, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Best RB, Schuler B. Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods. J. Am. Chem. Soc. 138 (36), 11714-11726 (2016)
• Aznauryan M, Delgado L, Soranno A, Nettels D, Huang JR, Labhardt AM, Grzesiek S, Schuler B. Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. Proc. Natl. Acad. Sci. USA 113 (37), E5389-E5398 (2016)
• Schuler B, Soranno A, Hofmann H, Nettels D. Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins. Annu. Rev. Biophys. 45, 207-231 (2016)

2015

• Borgia A, Kemplen KR, Borgia MB, Soranno A, Shammas S, Wunderlich B, Nettels D, Best RB, Clarke J, Schuler B. Transient misfolding dominates multidomain protein folding. Nat. Commun. 6, 8861 (2015)
• König I, Zarrine-Afsar A, Aznauryan M, Soranno A, Wunderlich B, Dingfelder F, Stüber JC, Plückthun A, Nettels D, Schuler B. Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells. Nat. Methods 12, 773-779 (2015)

2014

• Soranno A, Koenig I, Borgia MB, Hofmann H, Zosel F, Nettels D, Schuler B. Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments. Proc. Natl. Acad. Sci. USA 111 (13), 4874-4879 (2014)

2012

• Soranno A, Buchli B, Nettels D, Cheng RR, Müller-Späth S, Pfeil SH, Hoffmann A, Lipman EA, Makarov DE, Schuler B. Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. Proc. Natl. Acad. Sci. USA 109 (44), 17800-17806 (2012)
• Hofmann H, Soranno A, Borgia A, Gast K, Nettels D, Schuler B. Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy. Proc. Natl. Acad. Sci. USA 109 (40), 16155-16160 (2012)
• Borgia A, Wensley B, Soranno A, Nettels D, Borgia MB, Hoffmann A, Pfeil SH, Lipman EA, Clarke J, Schuler B. Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy. Nat. Commun. 3, 1195 (2012)
• Schuler B, Müller-Späth S, Soranno A, Nettels D. Application of Confocal Single-Molecule FRET to Intrinsically Disordered Proteins. In: Intrinsically Disordered Protein Analysis: Volume 2, Methods and Experimental Tools, Methods Mol. Biol. (2012)

2010

• Müller-Späth S*, Soranno A*, Hirschfeld V, Hofmann H, Rüegger S, Reymond L, Nettels D, Schuler B. Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc. Natl. Acad. Sci. USA 107 (33), 14609-14614 (2010)

2009

• Soranno A, Longhi R, Bellini T, Buscaglia M. Kinetics of Contact Formation and End-to-End Distance Distributions of Swollen Disordered Peptides. Biophys. J. 96 (4), 1515-1528 (2009)

Principal Investigator

Andrea Soranno, PhD
Associate Professor
Principal Investigator
soranno@wustl.edu

Faculty

Melissa D. Stuchell-Brereton, PhD
Assistant Professor
breretonm@wustl.edu

Staff Scientists

Jasmine Cubuk, PhD
Staff Scientist
cubukj@wustl.edu

Nirnay Samanta, PhD
Staff Scientist

Postdoctoral Researchers

Drake Jensen, PhD
Postdoctoral Researcher
drakejensen@wustl.edu

Graduate Students

Klaudio Fatmiri
PhD Student
Biochemistry, Biophysics, and Structural Biology
klaudio.f@wustl.edu

Madison Stringer
PhD Student
Biochemistry, Biophysics, and Structural Biology
m.a.stringer@wustl.edu

Anshuman Jaysingh
PhD Student
Biochemistry, Biophysics, and Structural Biology
a.jaysingh@wustl.edu

Ella Mozier
PhD Student
Biochemistry, Biophysics, and Structural Biology
Co-mentored with Dr. Michael Greenberg
e.i.mozier@wustl.edu

Eun Sil Rollins
PhD Student
Biochemistry, Biophysics, and Structural Biology
e.a.rollins@wustl.edu

Current Rotation Students

Daniel Sangiovanni
Rotation Student
Fall 2026

Cassandra Vance
Rotation Student
Fall 2026

Recent Rotation Students

Kevin Gery
BBSB Rotation Student
Fall 2026

Jacob McNally
BBSB Rotation Student
Fall 2026

Vincent Nicholson
BBSB Rotation Student
Fall 2025

Former Lab Members

Debjit Roy, PhD
Former Staff Scientist

Jhullian J. Alston, PhD
Former PhD Student, BBSB
Co-mentored with Dr. Alex Holehouse
Currently Postdoctoral Fellow, Taekjip Ha Lab, Boston Children’s Hospital / Harvard Medical School; HHMI Hanna Gray Fellow

J. Jeremias Incicco, PhD
Former Postdoctoral Fellow
Currently Investigador Asistente (Assistant Investigator) at CONICET/IQUIFIB, University of Buenos Aires, Argentina

Rashmi Karki, PhD
Former Research Technician
subsequently earned her PhD in BBSB at WashU (Garcia Lab), 2026

Owen Ouyang, PhD
Former Undergraduate Researcher
Currently Postdoctoral Scholar, Peter S. Kim Lab, Stanford University

Marco Todisco, PhD
Former Visiting PhD Student
University of Milan, Italy
Currently Postdoctoral Fellow, Ankur Jain Lab, Whitehead Institute

Pasquale Merolla
Former Visiting Master’s Student
University of Milan, Italy
Currently in the pharmaceutical industry, LEO Pharma, Copenhagen, Denmark

Logan Calderone
Former Undergraduate Researcher
Co-mentored by Dr. Melissa D. Stuchell-Brereton and Dr. Carl Frieden
PhD, Brandeis University, 2026

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.