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Protein and peptide folding, misfolding, and non-folding / ed. by Reinhard Schweitzer-Stenner
Contributor(s): Resource type: Ressourcentyp: Buch (Online)Book (Online)Language: English Series: Wiley series in protein and peptide science | Wiley Series in Protein and Peptide Science Ser ; v.13Publisher: Hoboken, N.J : John Wiley & Sons, c2012Edition: Online-AusgDescription: Online-Ressource (1 online resource (xxii, 548 p., [24] p. of plates)) : ill. (some col.)ISBN:- 9781280591778
- 1280591773
- 9781118183342
- 572.65
- 572/.633 23
- 572.633
- SCI049000
- QP551
Contents:
Summary: 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 singleSummary: Intro -- PROTEIN AND PEPTIDE FOLDING, MISFOLDING, AND NON-FOLDING -- CONTENTS -- INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE -- PREFACE -- CONTRIBUTORS -- INTRODUCTION -- 1: WHY ARE WE INTERESTED IN THE UNFOLDED PEPTIDES AND PROTEINS? Vladimir N. Uversky and A. Keith Dunker -- 1.1. INTRODUCTION -- 1.2. WHY STUDY IDPS? -- 1.3. LESSON 1: DISORDEREDNESS IS ENCODED IN THE AMINO ACID SEQUENCE AND CAN BE PREDICTED -- 1.4. LESSON 2: DISORDERED PROTEINS ARE HIGHLY ABUNDANT IN NATURE -- 1.5. LESSON 3: DISORDERED PROTEINS ARE GLOBALLY HETEROGENEOUS -- 1.6. LESSON 4: HYDRODYNAMIC DIMENSIONS OF NATIVELY UNFOLDED PROTEINS ARE CHARGE DEPENDENT -- 1.7. LESSON 5: POLYMER PHYSICS EXPLAINS HYDRODYNAMIC BEHAVIOR OF DISORDERED PROTEINS -- 1.8. LESSON 6: NATIVELY UNFOLDED PROTEINS ARE PLIABLE AND VERY SENSITIVE TO THEIR ENVIRONMENT -- 1.9. LESSON 7: WHEN BOUND, NATIVELY UNFOLDED PROTEINS CAN GAIN UNUSUAL STRUCTURES -- 1.10. LESSON 8: IDPS CAN FORM DISORDERED OR FUZZY COMPLEXES -- 1.11. LESSON 9: INTRINSIC DISORDER IS CRUCIAL FOR RECOGNITION, REGULATION, AND SIGNALING -- 1.12. LESSON 10: PROTEIN POSTTRANSLATIONAL MODIFICATIONS OCCUR AT DISORDERED REGIONS -- 1.13. LESSON 11: DISORDERED REGIONS ARE PRIMARY TARGETS FOR AS -- 1.14. LESSON 12: DISORDERED PROTEINS ARE TIGHTLY REGULATED IN THE LIVING CELLS -- 1.15. LESSON 13: NATIVELY UNFOLDED PROTEINS ARE FREQUENTLY ASSOCIATED WITH HUMAN DISEASES -- 1.16. LESSON 14: NATIVELY UNFOLDED PROTEINS ARE ATTRACTIVE DRUG TARGETS -- 1.17. LESSON 15: BRIGHT FUTURE OF FUZZY PROTEINS -- ACKNOWLEDGMENTS -- REFERENCES -- I: CONFORMATIONAL ANALYSISOF UNFOLDED STATES -- 2: EXPLORING THE ENERGY LANDSCAPE OF SMALL PEPTIDES AND PROTEINS BY MOLECULAR DYNAMICS SIMULATIONS Gerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen -- 2.1. INTRODUCTION: FREE ENERGY LANDSCAPES AND HOW TO CONSTRUCT THEM.PPN: PPN: 809672111Package identifier: Produktsigel: ZDB-26-MYL | ZDB-30-PAD | ZDB-30-PQE
""Series page""; ""Title page""; ""Copyright page""; ""INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE""; ""PREFACE""; ""CONTRIBUTORS""; ""INTRODUCTION""; ""1 WHY ARE WE INTERESTED IN THE UNFOLDED PEPTIDES AND PROTEINS?""; ""1.1. INTRODUCTION""; ""1.2. WHY STUDY IDPS?""; ""1.3. LESSON 1: DISORDEREDNESS IS ENCODED IN THE AMINO ACID SEQUENCE AND CAN BE PREDICTED""; ""1.4. LESSON 2: DISORDERED PROTEINS ARE HIGHLY ABUNDANT IN NATURE""; ""1.5. LESSON 3: DISORDERED PROTEINS ARE GLOBALLY HETEROGENEOUS""
""1.6. LESSON 4: HYDRODYNAMIC DIMENSIONS OF NATIVELY UNFOLDED PROTEINS ARE CHARGE DEPENDENT""""1.7. LESSON 5: POLYMER PHYSICS EXPLAINS HYDRODYNAMIC BEHAVIOR OF DISORDERED PROTEINS""; ""1.8. LESSON 6: NATIVELY UNFOLDED PROTEINS ARE PLIABLE AND VERY SENSITIVE TO THEIR ENVIRONMENT""; ""1.9. LESSON 7: WHEN BOUND, NATIVELY UNFOLDED PROTEINS CAN GAIN UNUSUAL STRUCTURES""; ""1.10. LESSON 8: IDPS CAN FORM DISORDERED OR FUZZY COMPLEXES""; ""1.11. LESSON 9: INTRINSIC DISORDER IS CRUCIAL FOR RECOGNITION, REGULATION, AND SIGNALING""
""1.12. LESSON 10: PROTEIN POSTTRANSLATIONAL MODIFICATIONS OCCUR AT DISORDERED REGIONS""""1.13. LESSON 11: DISORDERED REGIONS ARE PRIMARY TARGETS FOR AS""; ""1.14. LESSON 12: DISORDERED PROTEINS ARE TIGHTLY REGULATED IN THE LIVING CELLS""; ""1.15. LESSON 13: NATIVELY UNFOLDED PROTEINS ARE FREQUENTLY ASSOCIATED WITH HUMAN DISEASES""; ""1.16. LESSON 14: NATIVELY UNFOLDED PROTEINS ARE ATTRACTIVE DRUG TARGETS""; ""1.17. LESSON 15: BRIGHT FUTURE OF FUZZY PROTEINS""; ""ACKNOWLEDGMENTS""; ""I: CONFORMATIONAL ANALYSIS OF UNFOLDED STATES""
""2 EXPLORING THE ENERGY LANDSCAPE OF SMALL PEPTIDES AND PROTEINS BY MOLECULAR DYNAMICS SIMULATIONS""""2.1. INTRODUCTION: FREE ENERGY LANDSCAPES AND HOW TO CONSTRUCT THEM""; ""2.2. DIHEDRAL ANGLE PCA ALLOWS US TO SEPARATE INTERNAL AND GLOBAL MOTION""; ""2.3. DIMENSIONALITY OF THE FREE ENERGY LANDSCAPE""; ""2.4. CHARACTERIZATION OF THE FREE ENERGY LANDSCAPE: STATES, BARRIERS, AND TRANSITIONS""; ""2.5. LOW-DIMENSIONAL SIMULATION OF BIOMOLECULAR DYNAMICS TO CATCH SLOW AND RARE PROCESSES""; ""2.6. PCA BY PARTS: THE FOLDING PATHWAYS OF VILLIN HEADPIECE""
""2.7. THE ENERGY LANDSCAPE OF AGGREGATING Aβ-PEPTIDES""""2.8. CONCLUDING REMARKS""; ""ACKNOWLEDGMENTS""; ""3 LOCAL BACKBONE PREFERENCES AND NEAREST-NEIGHBOR EFFECTS IN THE UNFOLDED AND NATIVE STATES""; ""3.1. INTRODUCTION""; ""3.2. EARLY DAYS: RANDOM COILâ€"THEORY AND EXPERIMENT""; ""3.3. DENATURED PROTEINS AS SELF-AVOIDING RANDOM COILS""; ""3.4. MODELING THE UNFOLDED STATE""; ""3.5. NN EFFECTS IN PROTEIN STRUCTURE PREDICTION""; ""3.6. UTILIZING FOLDING PATHWAYS FOR STRUCTURE PREDICTION""; ""3.7. NATIVE STATE MODELING""
""3.8. SECONDARY-STRUCTURE PROPENSITIES: NATIVE BACKBONES IN UNFOLDED PROTEINS""
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