Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C
- 1st Edition, Volume 183 - October 14, 2021
- Imprint: Academic Press
- Editor: Vladimir N Uversky
- Language: English
- Hardback ISBN:9 7 8 - 0 - 3 2 3 - 8 5 2 9 9 - 9
- eBook ISBN:9 7 8 - 0 - 3 2 3 - 8 5 3 0 0 - 2
Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C, Volume 183 represents a set of selected studies on a variety of research topics re… Read more
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Request a sales quoteDancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C, Volume 183 represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins. Topics in this volume include discussions on the evolution of disorder, consideration of the peculiarities of phase separation of the prion protein, a general discussion of the relationships between intrinsic disorder and protein functions, coverage of the structural and functional characterization of several important intrinsically disordered proteins, such as transcription factors, outer membrane porins, trans-membrane and membrane associated proteins with ID regions, discussion of molecular simulations of IDPs, and much more.
- Provides recent studies on the intrinsically disordered proteins and their functions, along with the involvement of intrinsically disordered proteins in the pathogenesis of various diseases
- Contains numerous illustrative materials (color figures, diagrams and tables) to help readers delve into the information provided
- Includes contributions from recognized experts in the field
Scientists working in the fields of biochemistry, biophysics, molecular medicine, biotechnology, pharmacology and drug discovery, molecular and cellular biology, as well as students of Medical Schools, Departments of Biochemistry, Biophysics, Molecular Biology, Biotechnology, Cell Biology, etc. This book is of interest to everybody, who is fascinated by the protein intrinsic disorder phenomenon, including graduate students, postdoctoral students, and experienced researchers studying intrinsically disordered proteins (IDPs), their structures, and functions
- Cover image
- Title page
- Table of Contents
- Copyright
- Contributors
- Preface: The Patchwork Quilt of Intrinsic Disorder
- References
- Chapter One: Intrinsic disorder and phase transitions: Pieces in the puzzling role of the prion protein in health and disease
- Abstract
- 1: Introduction
- 2: Considerations on intrinsic disorder and phase separation ability of the prion protein family
- 3: The manifold interactions of PrP with nucleic acid targets: Can phase separation explain it?
- 4: Phase transitions of PrP in health and disease
- Acknowledgments
- References
- Chapter Two: Functions of intrinsically disordered proteins through evolutionary lenses
- Abstract
- 1: Introduction
- 2: Functional categories of IDPs
- 3: Distinct evolutionary scenarios of IDRs
- 4: Evolutionary conservation of SLIMs
- 5: Evolutionary origin IDRs mutated in cancer
- 6: Conclusion
- References
- Chapter Three: Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential
- Abstract
- References
- Chapter Four: Intrinsic disorder in integral membrane proteins
- Abstract
- 1: Distinction between intrinsically disordered and structured proteins
- 2: Intrinsic disorder in IMPs: Potential functional advantages
- 3: Mutations in IMP: Consideration of IDR
- 4: IMP intrinsic disorder: Investigational approaches
- 5: Conclusions
- References
- Chapter Five: Molecular simulations of IDPs: From ensemble generation to IDP interactions leading to disorder-to-order transitions
- Abstract
- 1: Introduction to IDPs
- 2: Force fields for IDPs
- 3: Simulation-based IDP ensemble generation and characterization
- 4: Modeling the disorder-to-order transition of IDPs
- 5: Summary and outlook
- References
- Chapter Six: Target-binding behavior of IDPs via pre-structured motifs
- Abstract
- 1: Introduction
- 2: Target-binding of IDPs
- 3: The pre-structured motif (PreSMo)
- 4: PreSMos in transcriptional and translational factors
- 5: PreSMos in neurodegenerative IDPs
- 6: PreSMos in other IDPs
- 7: Summary and perspective
- Acknowledgments
- References
- Chapter Seven: The role of dancing duplexes in biology and disease
- Abstract
- 1: Introduction
- 2: LC8-facilitated dimerization in IDP duplexes
- 3: Multivalent binding of LC8 along IDP duplexes
- 4: Nup159: A multivalent LC8 binder with a self-association domain
- 5: VSV-P: The role of disorder in a non-LC8 binding IDP duplex
- 6: The role of disorder and dimerization of the SARS-CoV-2 nucleocapsid phosphoprotein IDP duplex
- 7: Future directions
- 8: Conclusion
- References
- Chapter Eight: Intrinsic disorder in protein kinase A anchoring proteins signaling complexes
- Abstract
- 1: Tethered phosphorylation
- 2: Intrinsic disorder in PKA-AKAP signaling complexes
- 3: The prevalence of intrinsic disorder in AKAPs
- 4: Modeling the reach and effective concentration of PKA-AKAP signaling complexes
- 5: Allosteric regulation of tethered reactions by AKAP structure
- 6: Conclusions
- References
- Chapter Nine: Protein intrinsic disorder on a dynamic nucleosomal landscape
- Abstract
- 1: Introduction
- 2: Protein intrinsic disorder on a nucleosomal landscape
- 3: Disordered interactions with nucleosomes
- 4: Common sequence features of disordered nucleosome-binding proteins
- 5: Concluding remarks
- Acknowledgments
- References
- Chapter Ten: Flexible spandrels of the global plant virome: Proteomic-wide evolutionary patterns of structural intrinsic protein disorder elucidate modulation at the functional virus–host interplay
- Abstract
- 1: The highly modular plant virus proteome
- 2: Protein disorder composition in plant viruses: Terra incognita
- 3: The global plant virus proteome reveals overhauling IDP abundance and variability
- 4: General affinity of phylogenomically unrelated small plant virus proteomes with increased IDP
- 5: Emerging patterns in amino acid composition as a potential predictor of IDP and virus functional biology
- 6: The global plant virus MoRFome: Gaining functional insights in viral IDP-mediated binding contextual landscape via harnessing interface molecular recognition features
- 7: Evolutionary proteomic comparative analysis of conserved viral modules make up reveals IDP landscape of viral–host interacting disordomes
- 8: Functional IDP and evolutionary conserved structures expand evidence for modulation of transmission mode of plant viruses by insect vectors
- 9: Outlook and new challenging prospects for plant virology
- 10: Conclusion
- References
- Index
- Edition: 1
- Volume: 183
- Published: October 14, 2021
- No. of pages (Hardback): 434
- No. of pages (eBook): 434
- Imprint: Academic Press
- Language: English
- Hardback ISBN: 9780323852999
- eBook ISBN: 9780323853002
VU
Vladimir N Uversky
Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his PhD from Moscow Institute of Physics and Technology and D.Sc. from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. Since 2010, Professor Uversky has worked at University of South Florida, where he works on various aspects of protein intrinsic disorder phenomenon and analysis of protein folding and misfolding processes. He has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He also servs as an editor in a number of scientific journals.
Affiliations and expertise
Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United StatesRead Dancing Protein Clouds: Intrinsically Disordered Proteins in the Norm and Pathology, Part C on ScienceDirect