Osmolytes and Intrinsically Disordered Proteins: From Functional Regulation to Disease Pathogenesis, Volume 112 delves into the fascinating interplay between osmolytes and intrinsically disordered proteins (IDPs), exploring their pivotal roles in cellular function and disease mechanisms. This volume brings together experts to present cutting-edge research on how osmolytes regulate functional behavior of IDPs and ensure cellular stability and adaptability under stress conditions. Specific chapters cover Functional diversity of IDPs and their structural heterogeneity: Protein structure-function continuum, Osmolytes as structure-function regulators of intrinsically disordered casein, Synergism of the effects of osmolytes and crowders on structure and function of IDPs/IDRs: The natural habitat, and more.
Additional chapters delve into Osmolyte-IDP Interactions during Desiccation, Modulation of aggregation/fibrillation propensity of IDPs by osmolytes, Osmolytes in modulating the structural and functional integrity of α-synuclein: a study based on Parkinson's disease, Regulation of the structural dynamics, aggregation, and pathogenicity of polyQ-expanded Huntingtin by osmolytes, Aggregation and inhibitory strategies of amyloid fibrillation, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Copyright - p. iii 5. Contributors - p. iii 6. Preface - p. iii 7. Chapter One: Functional diversity of intrinsically disordered proteins and their structural heterogeneity: Protein structure-function continuum - p. iii 8. Chapter Two: Osmolytes as structure-function regulators of intrinsically disordered casein proteins - p. 18 9. Chapter Three: Osmolyte-IDP interactions during desiccation - p. 40 10. Chapter Four: Modulation of conformational integrity and aggregation propensity of α-synuclein by osmolytes: Implications in therapeutic intervention of Parkinson’s disease - p. 64 11. Chapter Five: Effect of osmolytes and posttranslational modifications on modulating the chaperone function of α-crystallin - p. 90 12. Chapter Six: Regulation of the structural dynamics, aggregation, and pathogenicity of polyQ-expanded Huntingtin by osmolytes - p. 114 13. Chapter Seven: Strategies for inhibiting amyloid fibrillation: Current status and future prospects - p. 146 14. Chapter Eight: The Huntington’s disease drug pipeline: a review of small molecules and their therapeutic targets - p. 170 15. Chapter Nine: Molecular crowding and amyloidogenic self-assembly: Emergent perspectives from modern computations - p. 210 16. Chapter Ten: Liquid-liquid phase separation of intrinsically disordered proteins: Effect of osmolytes and crowders - p. 250 17. Chapter Eleven: Factors responsible for alpha-Synuclein aggregation - p. 272 18. Index - p. 290
Osmolytes and Intrinsically Disordered Proteins: From Functional Regulation to Disease Pathogenesis, Volume 112 delves into the fascinating interplay between osmolytes and intrinsically disordered proteins (IDPs), exploring their pivotal roles in cellular function and disease mechanisms. This volume brings together experts to present cutting-edge research on how osmolytes regulate functional behavior of IDPs and ensure cellular stability and adaptability under stress conditions. Specific chapters cover Functional diversity of IDPs and their structural heterogeneity: Protein structure-function continuum, Osmolytes as structure-function regulators of intrinsically disordered casein, Synergism of the effects of osmolytes and crowders on structure and function of IDPs/IDRs: The natural habitat, and more.
Additional chapters delve into Osmolyte-IDP Interactions during Desiccation, Modulation of aggregation/fibrillation propensity of IDPs by osmolytes, Osmolytes in modulating the structural and functional integrity of α-synuclein: a study based on Parkinson's disease, Regulation of the structural dynamics, aggregation, and pathogenicity of polyQ-expanded Huntingtin by osmolytes, Aggregation and inhibitory strategies of amyloid fibrillation, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Copyright - p. iii 5. Contributors - p. iii 6. Preface - p. iii 7. Chapter One: Functional diversity of intrinsically disordered proteins and their structural heterogeneity: Protein structure-function continuum - p. iii 8. Chapter Two: Osmolytes as structure-function regulators of intrinsically disordered casein proteins - p. 18 9. Chapter Three: Osmolyte-IDP interactions during desiccation - p. 40 10. Chapter Four: Modulation of conformational integrity and aggregation propensity of α-synuclein by osmolytes: Implications in therapeutic intervention of Parkinson’s disease - p. 64 11. Chapter Five: Effect of osmolytes and posttranslational modifications on modulating the chaperone function of α-crystallin - p. 90 12. Chapter Six: Regulation of the structural dynamics, aggregation, and pathogenicity of polyQ-expanded Huntingtin by osmolytes - p. 114 13. Chapter Seven: Strategies for inhibiting amyloid fibrillation: Current status and future prospects - p. 146 14. Chapter Eight: The Huntington’s disease drug pipeline: a review of small molecules and their therapeutic targets - p. 170 15. Chapter Nine: Molecular crowding and amyloidogenic self-assembly: Emergent perspectives from modern computations - p. 210 16. Chapter Ten: Liquid-liquid phase separation of intrinsically disordered proteins: Effect of osmolytes and crowders - p. 250 17. Chapter Eleven: Factors responsible for alpha-Synuclein aggregation - p. 272 18. Index - p. 290
