Protein and Peptide Folding, Misfolding, and Non-Folding

Sheds new light on intrinsically disordered proteins andpeptides, including their role in neurodegenerative diseases

With the discovery of intrinsically disordered proteins andpeptides (IDPs), researchers realized that proteins do notnecessarily adopt a well defined secondary and tertiary structurein order to perform biological functions. In fact, IDPs playbiologically relevant roles, acting as inhibitors, scavengers, andeven facilitating DNA/RNA-protein interactions. Due to theirpropensity for self-aggregation and fibril formation, some IDPs areinvolved in neurodegenerative diseases such as Parkinson's andAlzheimer's.

With contributions from leading researchers, this text reviewsthe most recent studies, encapsulating our understanding of IDPs.The authors explain how the growing body of IDP research isbuilding our knowledge of the folding process, the binding ofligands to receptor molecules, and peptide self-aggregation.Readers will discover a variety of experimental, theoretical, andcomputational approaches used to better understand the propertiesand function of IDPs. Moreover, they'll discover the role of IDPsin human disease and as drug targets.

Protein and Peptide Folding, Misfolding, and Non-Folding beginswith an introduction that explains why research on IDPs hassignificantly expanded in the past few years. Next, the book isdivided into three sections:

• Conformational Analysis of Unfolded States

• Disordered Peptides and Molecular Recognition

• Aggregation of Disordered Peptides

Throughout the book, detailed figures help readers understandthe structure, properties, and function of IDPs. References at theend of each chapter serve as a gateway to the growing body ofliterature in the field.

With the publication of Protein and Peptide Folding, Misfolding, and Non-Folding, researchers now have a single place to discoverIDPs, their diverse biological functions, and the many disciplinesthat have contributed to our evolving understanding of them.