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.
Table des matières
A. Introduction
1. Why are we interested in the unfolded peptides and proteins?
Vladimir Uversky and Keith Dunker
B. Conformational analysis of unfolded states
2. Exploring the landscape of small peptides with MD simulations
Gerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen
3. Local backbone preferences and nearest neighbor effects in the unfolded and native states
Joe De Bartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick
4. Short-distance FRET applied to the polypeptide chain
Maik Jacob and Werner Nau
5. Solvation and electrostatics as determinants of conformational propensities in unfolded peptides and proteins
Franc Avbelji
6. Experimental and Computational Studies of Polyproline II Propensity
W. Austin Elam, Travis P. Schrank, Vincent J. Hilser
7. Mapping conformational dynamics in unfolded polypeptide chains using short model peptides by NMR spectroscopy
Daniel Mathieu, Karin Rybka, Jürgen Graf and Harald Schwalbe
8. Secondary Structure and Dynamics of a Family of Disordered Proteins
Pranesh Narayanaswami and Gary Daughdrill
C. Disordered Peptides and Molecular Recognition
9. Binding promiscuity of unfolded peptides
Christopher J. Oldfield, Bin Xue, A. Keith Dunker, and Vladimir N. Uversky
10. Intrinsic flexibility of nucleic acid chaperone proteins from pathogenic RNA viruses
Roland Ivanyi-Nagy, Zuzanna Makowska, and Jean-Luc Darlix
D. Aggregation of disordered peptides
11. Self-Assembling Alanine-Rich Peptides of Biomedical and Biotechnological Relevance
Thomas Measey and Reinhard Schweitzer-Stenner
12. Structural Elements Regulating Interactions in the Early Stages of Fibrillogenesis: A Human Calcitonin Model System
Rosa Maria Vitale, Giuseppina Andreotti, Pietro Amodeo, and Andrea Motta
13. Solution NMR Studies of Abeta Monomers and Oligomers
Chunyu Wang
14. Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins
Scott L. Crick and Rohit V. Pappu
15. Modifiers of protein aggregation – from non-specific to specific interactions
Michal Levy-Sakin, Roni Scherzer-Attali and Ehud Gazit
16. Computational Studies of Folding and Assembly of Amyloidogenic Proteins
J. Srinivasa Rao, Brigita Urbanc and Louis Cruz
A propos de l’auteur
Reinhard Schweitzer-Stenner, Ph D, is Professor and currently the Head of the Chemistry Department at Drexel University. Dr. Schweitzer-Stenner also heads the biospectroscopy research group. His research investigates peptide structure and functionally relevant heme distortions as well as ligand-receptor binding on the surface of mast cells. With more than 150 published research articles, Dr. Schweitzer-Stenner is widely recognized as a leader and pioneer in the study of the conformational properties of unfolded peptides.
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