Elizabeth Rhoades was born and raised in Huntsville, Alabama. As a child, she loved reading and when she left for college, she intended to major in English at Duke University. After taking a Physics course to fulfill a distribution requirement during her first year, she switched gears and decided to pursue a Physics major. In between her junior and senior years, she spent a summer at the University of Tennessee in a REU program, where she discovered biophysics. Liz earned her Ph.D. in 2001 from the Biophysics Research Division at the University of Michigan, working with Ari Gafni, a biophysical chemist, and Ducan Steel, a physicist, on understanding amyloid aggregation. It was in the Gafni-Steel lab that she became interested in understanding the physico-chemical basis of protein structure and dynamics and the power of fluorescence spectroscopy as a tool. She spent 2.5 years as a postdoctoral fellow with Gilad Haran at the Weizmann Institute, applying single molecule fluorescence to the study of protein folding, and then an additional 2.5 years as a postdoc in Watt Webb’s lab at Cornell University. In 2006, Liz joined the faculty in the Molecular Biophysics & Biochemistry Department at Yale University, where she rose through the academic ranks. She moved to the Chemistry Department at the University of Pennsylvania in 2016. In her independent career, her research focuses on understanding both functional and dysfunctional aspects of intrinsically disordered proteins, with a focus on several implicated in neurodegeneration. She has served as chair of the Intrinsically Disordered Protein Subgroup of the Biophysical Society and currently serves as Associate Editor of the Proteins section of the Biophysical Journal. Her husband is also a scientist/professor and she has two young sons who plan to be superheroes when they grow up.

• 1. Phase Separation of Intrinsically Disordered ProteinsAmmon E. Posey, Alex S. Holehouse and Rohit V. Pappu2. Methods and Strategies to Quantify Phase Separation of Disordered Proteins Alfredo Vidal Ceballos, Charles J. McDonald and Shana Elbaum-Garfinkle3. Visualization and Quantitation of Phase-Separated Droplet Formation by Human HP1αMadeline M. Keenen, Adam G. Larson and Geeta J. Narlikar4. Probing RNA Structure in Liquid–Liquid Phase Separation Using SHAPE-MaPErin M. Langdon and Amy S. Gladfelter5. The Use of 13C Direct-Detect NMR to Characterize Flexible and Disordered ProteinsErik C. Cook, Grace A. Usher and Scott A. Showalter6. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered ProteinsWade M. Borcherds and Gary W. Daughdrill7. Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional PartnersFrancesca Troilo, Christophe Bignon, Stefano Gianni, Monika Fuxreiter and Sonia Longhi8. Characterization of Dynamic IDP Complexes by NMR SpectroscopyAndreas Prestel, Katrine Bugge, Lasse Staby, Ruth Hendus-Altenburger and Birthe B. Kragelund9. Spectroscopic Characterization of Structure–Function Relationships in the Intrinsically Disordered Protein ComplexinDavid Snead and David Eliezer10. Distances, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRETErik D. Holmstrom, Andrea Holla, Wenwei Zheng, Daniel Nettles, Robert B. Best and Benjamin Schuler11. Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRETPiau Siong Tan and Edward A. Lemke12. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered ProteinsAnupa Majumdar and Samrat Mukhopadhyay13. Building, Characterization, and Applications of Cuvette-FCS in Denaturant-Induced Expansion of Globular and Disordered ProteinsTimir Baran Sil, Bankanidhi Sahoo and Kanchan Garai14. Stopped-Flow Kinetic Techniques for Studying Binding Reactions of Intrinsically Disordered ProteinsMichael D. Crabtree and Sarah L. Shammas15. The Use of Mass Spectrometry to Examine IDPs: Unique Insights and CaveatsDale Stuchfield, Aidan France, Lukasz G. Migas, Anja Thalhammer, Anne Bremer, Bruno Bellina and Perdita E. Barran16. Characterizing Time-of-Day Conformational Changes in the Intrinsically Disordered Proteins of the Circadian ClockJacqueline F. Pelham, Alexander E. Mosier and Jennifer M. Hurley17. Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric ModelJing Li and Vincent J. Hilser18. A Tethered Vesicle Assay for High-Throughput Quantification of Membrane FissionWilton T. Snead and Jeanne C. Stachowiak19. Generating Novel Materials Using the Intrinsically Disordered Protein UbxGabriela Geraldo Mendes, Rebecca M. Booth, Donna L. Pattison, Adrian J. Alvarez and Sarah E. Bondos20. Challenges in the Structural–Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody ToolsAngela Bekesi, Sara Abdellaoui, Natalie Holroyd, Wouter Van Delm, Els Pardon, Jarne Pauwels, Kris Gevaert, Jan Steyaert, Stefaan Derveaux, Antoni Borysik and Peter Tompa21. Characterization of the Binding of Small Molecules to Intrinsically Disordered ProteinsVeselin S. Dobrev, Lisette M. Fred, Kaitlyn P. Gerhart and Steven J. Metallo22. Targeting the Intrinsically Disordered Proteome Using Small Molecule LigandsSławomir Wójcik, Melissa Birol, Elizabeth Rhoades, Andrew D. Miranker and Zachary A. Levine

Elizabeth Rhoades was born and raised in Huntsville, Alabama. As a child, she loved reading and when she left for college, she intended to major in English at Duke University. After taking a Physics course to fulfill a distribution requirement during her first year, she switched gears and decided to pursue a Physics major. In between her junior and senior years, she spent a summer at the University of Tennessee in a REU program, where she discovered biophysics. Liz earned her Ph.D. in 2001 from the Biophysics Research Division at the University of Michigan, working with Ari Gafni, a biophysical chemist, and Ducan Steel, a physicist, on understanding amyloid aggregation. It was in the Gafni-Steel lab that she became interested in understanding the physico-chemical basis of protein structure and dynamics and the power of fluorescence spectroscopy as a tool. She spent 2.5 years as a postdoctoral fellow with Gilad Haran at the Weizmann Institute, applying single molecule fluorescence to the study of protein folding, and then an additional 2.5 years as a postdoc in Watt Webb’s lab at Cornell University. In 2006, Liz joined the faculty in the Molecular Biophysics & Biochemistry Department at Yale University, where she rose through the academic ranks. She moved to the Chemistry Department at the University of Pennsylvania in 2016. In her independent career, her research focuses on understanding both functional and dysfunctional aspects of intrinsically disordered proteins, with a focus on several implicated in neurodegeneration. She has served as chair of the Intrinsically Disordered Protein Subgroup of the Biophysical Society and currently serves as Associate Editor of the Proteins section of the Biophysical Journal. Her husband is also a scientist/professor and she has two young sons who plan to be superheroes when they grow up.

• 1. Phase Separation of Intrinsically Disordered ProteinsAmmon E. Posey, Alex S. Holehouse and Rohit V. Pappu2. Methods and Strategies to Quantify Phase Separation of Disordered Proteins Alfredo Vidal Ceballos, Charles J. McDonald and Shana Elbaum-Garfinkle3. Visualization and Quantitation of Phase-Separated Droplet Formation by Human HP1αMadeline M. Keenen, Adam G. Larson and Geeta J. Narlikar4. Probing RNA Structure in Liquid–Liquid Phase Separation Using SHAPE-MaPErin M. Langdon and Amy S. Gladfelter5. The Use of 13C Direct-Detect NMR to Characterize Flexible and Disordered ProteinsErik C. Cook, Grace A. Usher and Scott A. Showalter6. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered ProteinsWade M. Borcherds and Gary W. Daughdrill7. Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional PartnersFrancesca Troilo, Christophe Bignon, Stefano Gianni, Monika Fuxreiter and Sonia Longhi8. Characterization of Dynamic IDP Complexes by NMR SpectroscopyAndreas Prestel, Katrine Bugge, Lasse Staby, Ruth Hendus-Altenburger and Birthe B. Kragelund9. Spectroscopic Characterization of Structure–Function Relationships in the Intrinsically Disordered Protein ComplexinDavid Snead and David Eliezer10. Distances, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRETErik D. Holmstrom, Andrea Holla, Wenwei Zheng, Daniel Nettles, Robert B. Best and Benjamin Schuler11. Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRETPiau Siong Tan and Edward A. Lemke12. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered ProteinsAnupa Majumdar and Samrat Mukhopadhyay13. Building, Characterization, and Applications of Cuvette-FCS in Denaturant-Induced Expansion of Globular and Disordered ProteinsTimir Baran Sil, Bankanidhi Sahoo and Kanchan Garai14. Stopped-Flow Kinetic Techniques for Studying Binding Reactions of Intrinsically Disordered ProteinsMichael D. Crabtree and Sarah L. Shammas15. The Use of Mass Spectrometry to Examine IDPs: Unique Insights and CaveatsDale Stuchfield, Aidan France, Lukasz G. Migas, Anja Thalhammer, Anne Bremer, Bruno Bellina and Perdita E. Barran16. Characterizing Time-of-Day Conformational Changes in the Intrinsically Disordered Proteins of the Circadian ClockJacqueline F. Pelham, Alexander E. Mosier and Jennifer M. Hurley17. Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric ModelJing Li and Vincent J. Hilser18. A Tethered Vesicle Assay for High-Throughput Quantification of Membrane FissionWilton T. Snead and Jeanne C. Stachowiak19. Generating Novel Materials Using the Intrinsically Disordered Protein UbxGabriela Geraldo Mendes, Rebecca M. Booth, Donna L. Pattison, Adrian J. Alvarez and Sarah E. Bondos20. Challenges in the Structural–Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody ToolsAngela Bekesi, Sara Abdellaoui, Natalie Holroyd, Wouter Van Delm, Els Pardon, Jarne Pauwels, Kris Gevaert, Jan Steyaert, Stefaan Derveaux, Antoni Borysik and Peter Tompa21. Characterization of the Binding of Small Molecules to Intrinsically Disordered ProteinsVeselin S. Dobrev, Lisette M. Fred, Kaitlyn P. Gerhart and Steven J. Metallo22. Targeting the Intrinsically Disordered Proteome Using Small Molecule LigandsSławomir Wójcik, Melissa Birol, Elizabeth Rhoades, Andrew D. Miranker and Zachary A. Levine

Elizabeth Rhoades was born and raised in Huntsville, Alabama. As a child, she loved reading and when she left for college, she intended to major in English at Duke University. After taking a Physics course to fulfill a distribution requirement during her first year, she switched gears and decided to pursue a Physics major. In between her junior and senior years, she spent a summer at the University of Tennessee in a REU program, where she discovered biophysics. Liz earned her Ph.D. in 2001 from the Biophysics Research Division at the University of Michigan, working with Ari Gafni, a biophysical chemist, and Ducan Steel, a physicist, on understanding amyloid aggregation. It was in the Gafni-Steel lab that she became interested in understanding the physico-chemical basis of protein structure and dynamics and the power of fluorescence spectroscopy as a tool. She spent 2.5 years as a postdoctoral fellow with Gilad Haran at the Weizmann Institute, applying single molecule fluorescence to the study of protein folding, and then an additional 2.5 years as a postdoc in Watt Webb’s lab at Cornell University. In 2006, Liz joined the faculty in the Molecular Biophysics & Biochemistry Department at Yale University, where she rose through the academic ranks. She moved to the Chemistry Department at the University of Pennsylvania in 2016. In her independent career, her research focuses on understanding both functional and dysfunctional aspects of intrinsically disordered proteins, with a focus on several implicated in neurodegeneration. She has served as chair of the Intrinsically Disordered Protein Subgroup of the Biophysical Society and currently serves as Associate Editor of the Proteins section of the Biophysical Journal. Her husband is also a scientist/professor and she has two young sons who plan to be superheroes when they grow up.

• 1. Phase Separation of Intrinsically Disordered ProteinsAmmon E. Posey, Alex S. Holehouse and Rohit V. Pappu2. Methods and Strategies to Quantify Phase Separation of Disordered Proteins Alfredo Vidal Ceballos, Charles J. McDonald and Shana Elbaum-Garfinkle3. Visualization and Quantitation of Phase-Separated Droplet Formation by Human HP1αMadeline M. Keenen, Adam G. Larson and Geeta J. Narlikar4. Probing RNA Structure in Liquid–Liquid Phase Separation Using SHAPE-MaPErin M. Langdon and Amy S. Gladfelter5. The Use of 13C Direct-Detect NMR to Characterize Flexible and Disordered ProteinsErik C. Cook, Grace A. Usher and Scott A. Showalter6. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered ProteinsWade M. Borcherds and Gary W. Daughdrill7. Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional PartnersFrancesca Troilo, Christophe Bignon, Stefano Gianni, Monika Fuxreiter and Sonia Longhi8. Characterization of Dynamic IDP Complexes by NMR SpectroscopyAndreas Prestel, Katrine Bugge, Lasse Staby, Ruth Hendus-Altenburger and Birthe B. Kragelund9. Spectroscopic Characterization of Structure–Function Relationships in the Intrinsically Disordered Protein ComplexinDavid Snead and David Eliezer10. Distances, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRETErik D. Holmstrom, Andrea Holla, Wenwei Zheng, Daniel Nettles, Robert B. Best and Benjamin Schuler11. Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRETPiau Siong Tan and Edward A. Lemke12. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered ProteinsAnupa Majumdar and Samrat Mukhopadhyay13. Building, Characterization, and Applications of Cuvette-FCS in Denaturant-Induced Expansion of Globular and Disordered ProteinsTimir Baran Sil, Bankanidhi Sahoo and Kanchan Garai14. Stopped-Flow Kinetic Techniques for Studying Binding Reactions of Intrinsically Disordered ProteinsMichael D. Crabtree and Sarah L. Shammas15. The Use of Mass Spectrometry to Examine IDPs: Unique Insights and CaveatsDale Stuchfield, Aidan France, Lukasz G. Migas, Anja Thalhammer, Anne Bremer, Bruno Bellina and Perdita E. Barran16. Characterizing Time-of-Day Conformational Changes in the Intrinsically Disordered Proteins of the Circadian ClockJacqueline F. Pelham, Alexander E. Mosier and Jennifer M. Hurley17. Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric ModelJing Li and Vincent J. Hilser18. A Tethered Vesicle Assay for High-Throughput Quantification of Membrane FissionWilton T. Snead and Jeanne C. Stachowiak19. Generating Novel Materials Using the Intrinsically Disordered Protein UbxGabriela Geraldo Mendes, Rebecca M. Booth, Donna L. Pattison, Adrian J. Alvarez and Sarah E. Bondos20. Challenges in the Structural–Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody ToolsAngela Bekesi, Sara Abdellaoui, Natalie Holroyd, Wouter Van Delm, Els Pardon, Jarne Pauwels, Kris Gevaert, Jan Steyaert, Stefaan Derveaux, Antoni Borysik and Peter Tompa21. Characterization of the Binding of Small Molecules to Intrinsically Disordered ProteinsVeselin S. Dobrev, Lisette M. Fred, Kaitlyn P. Gerhart and Steven J. Metallo22. Targeting the Intrinsically Disordered Proteome Using Small Molecule LigandsSławomir Wójcik, Melissa Birol, Elizabeth Rhoades, Andrew D. Miranker and Zachary A. Levine