Intrinsically Disordered Proteins
- 1st Edition, Volume 611 - November 26, 2018
- Latest edition
- Editor: Elizabeth Rhoades
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 8 1 5 6 4 9 - 0
- eBook ISBN:9 7 8 - 0 - 1 2 - 8 1 5 6 5 0 - 6
Intrinsically Disordered Proteins, Volume 611, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting inter… Read more
Intrinsically Disordered Proteins, Volume 611, the latest release in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics of interest, including the Characterization of Structure-Function relationships in the intrinsically disordered protein complexin, Distances, distance distributions, and ensembles of IDPs from single-molecule FRET, Biophysical characterization of disordered protein liquid phases, The Use of Mass Spectrometry to Examine IDPs – Unique Insights and Caveats, Fluorescence Depolarization Kinetics to Study Conformational Preference, Structural Plasticity and Membrane Binding of Intrinsically Disordered Proteins, Characterizing the Function of Intrinsically Disordered Proteins in the Circadian Clock, and more.
- Breadth of experimental approaches and systems that will be covered
- The expertise of the contributors writing the articles
Basic research scientists – biophysicists, biochemists, and biologists – who are studying systems where protein disorder is important to function or dysfunction.
1. Phase Separation of Intrinsically Disordered Proteins
Ammon E. Posey, Alex S. Holehouse and Rohit V. Pappu
2. Methods and Strategies to Quantify Phase Separation of Disordered Proteins
Alfredo Vidal Ceballos, Charles J. McDonald and Shana Elbaum-Garfinkle
3. Visualization and Quantitation of Phase-Separated Droplet Formation by Human HP1α
Madeline M. Keenen, Adam G. Larson and Geeta J. Narlikar
4. Probing RNA Structure in Liquid–Liquid Phase Separation Using SHAPE-MaP
Erin M. Langdon and Amy S. Gladfelter
5. The Use of 13C Direct-Detect NMR to Characterize Flexible and Disordered Proteins
Erik C. Cook, Grace A. Usher and Scott A. Showalter
6. Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins
Wade M. Borcherds and Gary W. Daughdrill
7. Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners
Francesca Troilo, Christophe Bignon, Stefano Gianni, Monika Fuxreiter and Sonia Longhi
8. Characterization of Dynamic IDP Complexes by NMR Spectroscopy
Andreas Prestel, Katrine Bugge, Lasse Staby, Ruth Hendus-Altenburger and Birthe B. Kragelund
9. Spectroscopic Characterization of Structure–Function Relationships in the Intrinsically Disordered Protein Complexin
David Snead and David Eliezer
10. Distances, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRET
Erik D. Holmstrom, Andrea Holla, Wenwei Zheng, Daniel Nettles, Robert B. Best and Benjamin Schuler
11. Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET
Piau Siong Tan and Edward A. Lemke
12. Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered Proteins
Anupa Majumdar and Samrat Mukhopadhyay
13. Building, Characterization, and Applications of Cuvette-FCS in Denaturant-Induced Expansion of Globular and Disordered Proteins
Timir Baran Sil, Bankanidhi Sahoo and Kanchan Garai
14. Stopped-Flow Kinetic Techniques for Studying Binding Reactions of Intrinsically Disordered Proteins
Michael D. Crabtree and Sarah L. Shammas
15. The Use of Mass Spectrometry to Examine IDPs: Unique Insights and Caveats
Dale Stuchfield, Aidan France, Lukasz G. Migas, Anja Thalhammer, Anne Bremer, Bruno Bellina and Perdita E. Barran
16. Characterizing Time-of-Day Conformational Changes in the Intrinsically Disordered Proteins of the Circadian Clock
Jacqueline F. Pelham, Alexander E. Mosier and Jennifer M. Hurley
17. Assessing Allostery in Intrinsically Disordered Proteins With Ensemble Allosteric Model
Jing Li and Vincent J. Hilser
18. A Tethered Vesicle Assay for High-Throughput Quantification of Membrane Fission
Wilton T. Snead and Jeanne C. Stachowiak
19. Generating Novel Materials Using the Intrinsically Disordered Protein Ubx
Gabriela Geraldo Mendes, Rebecca M. Booth, Donna L. Pattison, Adrian J. Alvarez and Sarah E. Bondos
20. Challenges in the Structural–Functional Characterization of Multidomain, Partially Disordered Proteins CBP and p300: Preparing Native Proteins and Developing Nanobody Tools
Angela Bekesi, Sara Abdellaoui, Natalie Holroyd, Wouter Van Delm, Els Pardon, Jarne Pauwels, Kris Gevaert, Jan Steyaert, Stefaan Derveaux, Antoni Borysik and Peter Tompa
21. Characterization of the Binding of Small Molecules to Intrinsically Disordered Proteins
Veselin S. Dobrev, Lisette M. Fred, Kaitlyn P. Gerhart and Steven J. Metallo
22. Targeting the Intrinsically Disordered Proteome Using Small Molecule Ligands
Sławomir Wójcik, Melissa Birol, Elizabeth Rhoades, Andrew D. Miranker and Zachary A. Levine
- Edition: 1
- Latest edition
- Volume: 611
- Published: November 26, 2018
- Language: English
ER
Elizabeth Rhoades
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.
Affiliations and expertise
Associate Professor, Department of Chemistry, University of Pennsylvania, Philadelphia, PA, USARead Intrinsically Disordered Proteins on ScienceDirect