Wiley, 2012. - 583 p. - Sheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseases. With the discovery of intrinsically disordered proteins and peptides (IDPs), researchers realized that proteins do not necessarily adopt a well defined secondary and tertiary structure in order to perform biological functions. In fact, IDPs play biologically relevant roles, acting as inhibitors, scavengers, and even facilitating DNA/RNA-protein interactions. Due to their propensity for self-aggregation and fibril formation, some IDPs are involved in neurodegenerative diseases such as Parkinson's and Alzheimer's. With contributions from leading researchers, this text reviews the most recent studies, encapsulating our understanding of IDPs. The authors explain how the growing body of IDP research is building our knowledge of the folding process, the binding of ligands to receptor molecules, and peptide self-aggregation. Readers will discover a variety of experimental, theoretical, and computational approaches used to better understand the properties and function of IDPs. Moreover, they'll discover the role of IDPs in human disease and as drug targets. Protein and Peptide Folding, Misfolding, and Non-Folding begins with an introduction that explains why research on IDPs has significantly expanded in the past few years. Next, the book is divided into three sections:
- Conformational Analysis of Unfolded States
- Disordered Peptides and Molecular Recognition
- Aggregation of Disordered Peptides
Throughout the book, detailed figures help readers understand the structure, properties, and function of IDPs. References at the end of each chapter serve as a gateway to the growing body of literature in the field. With the publication of Protein and Peptide Folding, Misfolding, and Non-Folding, researchers now have a single place to discover IDPs, their diverse biological functions, and the many disciplines that have contributed to our evolving understanding of them.Contents
Introduction to the Wiley Series on Protein and Peptide Science
Preface
Contributors
Introduction
Why Are We Interested in the Unfolded Peptides and Proteins?
Exploring the Energy Landscape of Small Peptides and Proteins by Molecular Dynamics Simulations
Local Backbone Preferences and Nearest-Neighbor Effects in the Unfolded and Native States
Short-Distance FRET Applied to the Polypeptide Chain
Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins
Experimental and Computational Studies of Polyproline II Propensity
Mapping Conformational Dynamics in Unfolded Polypeptide Chains Using Short Model Peptides by NMR Spectroscopy
Secondary Structure and Dynamics of a Family of Disordered Proteins
Binding Promiscuity of Unfolded Peptides
Intrinsic Flexibility of Nucleic Acid Chaperone Proteins from Pathogenic RNA Viruses
Self-Assembling Alanine-Rich Peptides of Biomedical and Biotechnological Relevance
Structural Elements Regulating Interactions in the Early Stages of Fibrillogenesis: A Human Calcitonin Model System
Solution NMR Studies of Aβ Monomers and Oligomers
Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins
Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions
Computational Studies of Folding and Assembly of Amyloidogenic Proteins
Index
