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Protein and Peptide Folding, Misfolding, and Non-Folding als Buch (gebunden)
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Protein and Peptide Folding, Misfolding, and Non-Folding

'Wiley Series in Protein and Peptide Science'. 1. Auflage. Sprache: Englisch.
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This book provides an overview on what researchers have learned about unfolded peptides and how this knowledge facilitates the understanding of (a) the folding process, (b) the binding of ligands to receptor molecules, and (c) peptide self-aggregatio … weiterlesen
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Protein and Peptide Folding, Misfolding, and Non-Folding als Buch (gebunden)

Produktdetails

Titel: Protein and Peptide Folding, Misfolding, and Non-Folding
Autor/en: Vladimir Uversky, Reinhard Schweitzer-Stenner

ISBN: 0470591692
EAN: 9780470591697
'Wiley Series in Protein and Peptide Science'.
1. Auflage.
Sprache: Englisch.
Herausgegeben von Reinhard Schweitzer-Stenner, Vladimir Uversky
Wiley-Blackwell

10. April 2012 - gebunden - 576 Seiten

Beschreibung

This book provides an overview on what researchers have learned about unfolded peptides and how this knowledge facilitates the understanding of (a) the folding process, (b) the binding of ligands to receptor molecules, and (c) peptide self-aggregation. In this context, different experimental, theoretical, and computational concepts and approaches are introduced. This book can become a very useful addition for graduate-level courses on protein folding for the education of undergraduate and graduate students in research groups, which are exploring peptide self-aggregation for biomedical and biotechnological purposes. 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.

Inhaltsverzeichnis

Introduction to the Wiley Series on Protein and Peptide Science xiii

Preface xv

Contributors xix

INTRODUCTION 1

1 Why Are We Interested in the Unfolded Peptides and Proteins? 3
Vladimir N. Uversky and A. Keith Dunker

1.1 Introduction, 3

1.2 Why Study IDPs?, 4

1.3 Lesson 1: Disorderedness Is Encoded in the Amino Acid Sequence and Can Be Predicted, 5

1.4 Lesson 2: Disordered Proteins Are Highly Abundant in Nature, 7

1.5 Lesson 3: Disordered Proteins Are Globally Heterogeneous, 9

1.6 Lesson 4: Hydrodynamic Dimensions of Natively Unfolded Proteins Are Charge Dependent, 14

1.7 Lesson 5: Polymer Physics Explains Hydrodynamic Behavior of Disordered Proteins, 16

1.8 Lesson 6: Natively Unfolded Proteins Are Pliable and Very Sensitive to Their Environment, 18

1.9 Lesson 7: When Bound, Natively Unfolded Proteins Can Gain Unusual Structures, 20

1.10 Lesson 8: IDPs Can Form Disordered or Fuzzy Complexes, 25

1.11 Lesson 9: Intrinsic Disorder Is Crucial for Recognition, Regulation, and Signaling, 25

1.12 Lesson 10: Protein Posttranslational Modifi cations Occur at Disordered Regions, 28

1.13 Lesson 11: Disordered Regions Are Primary Targets for AS, 30

1.14 Lesson 12: Disordered Proteins Are Tightly Regulated in the Living Cells, 31

1.15 Lesson 13: Natively Unfolded Proteins Are Frequently Associated with Human Diseases, 33

1.16 Lesson 14: Natively Unfolded Proteins Are Attractive Drug Targets, 35

1.17 Lesson 15: Bright Future of Fuzzy Proteins, 38

Acknowledgments, 39

References, 40

I CONFORMATIONAL ANALYSIS OF UNFOLDED STATES 55

2 Exploring the Energy Landscape of Small Peptides and Proteins by Molecular Dynamics Simulations 57
Gerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen

2.1 Introduction: Free Energy Landscapes and How to Construct Them, 57

2.2 Dihedral Angle PCA Allows Us to Separate Internal and Global Motion, 61

2.3 Dimensionality of the Free Energy Landscape, 62

2.4 Characterization of the Free Energy Landscape: States, Barriers, and Transitions, 65

2.5 Low-Dimensional Simulation of Biomolecular Dynamics to Catch Slow and Rare Processes, 67

2.6 PCA by Parts: The Folding Pathways of Villin Headpiece, 69

2.7 The Energy Landscape of Aggregating A²-Peptides, 73

2.8 Concluding Remarks, 74

Acknowledgments, 75

References, 75

3 Local Backbone Preferences and Nearest-Neighbor Effects in the Unfolded and Native States 79
Joe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick

3.1 Introduction, 79

3.2 Early Days: Random Coil--Theory and Experiment, 80

3.3 Denatured Proteins as Self-Avoiding Random Coils, 82

3.4 Modeling the Unfolded State, 82

3.5 NN Effects in Protein Structure Prediction, 86

3.6 Utilizing Folding Pathways for Structure Prediction, 87

3.7 Native State Modeling, 88

3.8 Secondary-Structure Propensities: Native Backbones in Unfolded Proteins, 92

3.9 Conclusions, 92

Acknowledgments, 93

References, 94

4 Short-Distance FRET Applied to the Polypeptide Chain 99
Maik H. Jacob and Werner M. Nau

4.1 A Short Timeline of Resonance Energy Transfer Applied to the Polypeptide Chain, 99

4.2 A Short Theory of FRET Applied to the Polypeptide Chain, 101

4.3 DBO and Dbo, 105

4.4 Short-Distance FRET Applied to the Structured Polypeptide Chain, 107

4.5 Short-Distance FRET to Monitor Chain-Structural Transitions upon Phosphorylation, 116

4.6 Short-Distance FRET Applied to the Structureless Chain, 120

4.7 The Future of Short-Distance FRET, 125

Acknowledgments, 125

Dedication, 126

References, 126

5 Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins 131
Franc Avbelj

5.1 Local Structural Order in Unfolded Peptides and Proteins, 131

5.2 ESM, 134

5.3 The ESM and Strand-Coil Transition Model, 137

5.4 The ESM and Backbone Conformational Preferences, 138

5.5 The Nearest-Neighbor Effect,

Portrait

Reinhard Schweitzer-Stenner, PhD, 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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