{"product_id":"protein-and-peptide-folding-misfolding-and-non-folding-isbn-9780470591697","title":"Protein and Peptide Folding, Misfolding, and Non-Folding","description":"\u003cp\u003eSheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseases\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e \u003cp\u003eProtein 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:\u003c\/p\u003e \u003cul\u003e \u003cli\u003e \u003cp\u003eConformational Analysis of Unfolded States\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eDisordered Peptides and Molecular Recognition\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eAggregation of Disordered Peptides\u003c\/p\u003e \u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eThroughout 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.\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e  \u003cb\u003eIntroduction to the \u003ci\u003eWiley Series on Protein and Peptide Science\u003c\/i\u003e xiii\u003c\/b\u003e  \u003cp\u003e\u003cb\u003ePreface xv\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eContributors xix\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eINTRODUCTION 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Why Are We Interested in the Unfolded Peptides and Proteins? 3\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eVladimir N. Uversky and A. Keith Dunker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction, 3\u003c\/p\u003e \u003cp\u003e1.2 Why Study IDPs?, 4\u003c\/p\u003e \u003cp\u003e1.3 \u003ci\u003eLesson 1\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Disorderedness Is Encoded in the Amino Acid Sequence and Can Be Predicted, 5\u003c\/p\u003e \u003cp\u003e1.4 \u003ci\u003eLesson 2\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Disordered Proteins Are Highly Abundant in Nature, 7\u003c\/p\u003e \u003cp\u003e1.5 \u003ci\u003eLesson 3\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Disordered Proteins Are Globally Heterogeneous, 9\u003c\/p\u003e \u003cp\u003e1.6 \u003ci\u003eLesson 4\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Hydrodynamic Dimensions of Natively Unfolded Proteins Are Charge Dependent, 14\u003c\/p\u003e \u003cp\u003e1.7 \u003ci\u003eLesson 5\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Polymer Physics Explains Hydrodynamic Behavior of Disordered Proteins, 16\u003c\/p\u003e \u003cp\u003e1.8 \u003ci\u003eLesson 6\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Natively Unfolded Proteins Are Pliable and Very Sensitive to Their Environment, 18\u003c\/p\u003e \u003cp\u003e1.9 \u003ci\u003eLesson 7\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e When Bound, Natively Unfolded Proteins Can Gain Unusual Structures, 20\u003c\/p\u003e \u003cp\u003e1.10 \u003ci\u003eLesson 8\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e IDPs Can Form Disordered or Fuzzy Complexes, 25\u003c\/p\u003e \u003cp\u003e1.11 \u003ci\u003eLesson 9\u003cb\u003e:\u003c\/b\u003e\u003c\/i\u003e Intrinsic Disorder Is Crucial for Recognition, Regulation, and Signaling, 25\u003c\/p\u003e \u003cp\u003e1.12 \u003ci\u003eLesson 10:\u003c\/i\u003e Protein Posttranslational Modifi cations Occur at Disordered Regions, 28\u003c\/p\u003e \u003cp\u003e1.13 \u003ci\u003eLesson 11:\u003c\/i\u003e Disordered Regions Are Primary Targets for AS, 30\u003c\/p\u003e \u003cp\u003e1.14 \u003ci\u003eLesson 12:\u003c\/i\u003e Disordered Proteins Are Tightly Regulated in the Living Cells, 31\u003c\/p\u003e \u003cp\u003e1.15 \u003ci\u003eLesson 13:\u003c\/i\u003e Natively Unfolded Proteins Are Frequently Associated with Human Diseases, 33\u003c\/p\u003e \u003cp\u003e1.16 \u003ci\u003eLesson 14:\u003c\/i\u003e Natively Unfolded Proteins Are Attractive Drug Targets, 35\u003c\/p\u003e \u003cp\u003e1.17 \u003ci\u003eLesson 15:\u003c\/i\u003e Bright Future of Fuzzy Proteins, 38\u003c\/p\u003e \u003cp\u003eAcknowledgments, 39\u003c\/p\u003e \u003cp\u003eReferences, 40\u003c\/p\u003e \u003cp\u003e\u003cb\u003eI CONFORMATIONAL ANALYSIS OF UNFOLDED STATES 55\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Exploring the Energy Landscape of Small Peptides and Proteins by Molecular Dynamics Simulations 57\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eGerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction: Free Energy Landscapes and How to Construct Them, 57\u003c\/p\u003e \u003cp\u003e2.2 Dihedral Angle PCA Allows Us to Separate Internal and Global Motion, 61\u003c\/p\u003e \u003cp\u003e2.3 Dimensionality of the Free Energy Landscape, 62\u003c\/p\u003e \u003cp\u003e2.4 Characterization of the Free Energy Landscape: States, Barriers, and Transitions, 65\u003c\/p\u003e \u003cp\u003e2.5 Low-Dimensional Simulation of Biomolecular Dynamics to Catch Slow and Rare Processes, 67\u003c\/p\u003e \u003cp\u003e2.6 PCA by Parts: The Folding Pathways of Villin Headpiece, 69\u003c\/p\u003e \u003cp\u003e2.7 The Energy Landscape of Aggregating A\u003ci\u003eβ\u003c\/i\u003e-Peptides, 73\u003c\/p\u003e \u003cp\u003e2.8 Concluding Remarks, 74\u003c\/p\u003e \u003cp\u003eAcknowledgments, 75\u003c\/p\u003e \u003cp\u003eReferences, 75\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Local Backbone Preferences and Nearest-Neighbor Effects in the Unfolded and Native States 79\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJoe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction, 79\u003c\/p\u003e \u003cp\u003e3.2 Early Days: Random Coil—Theory and Experiment, 80\u003c\/p\u003e \u003cp\u003e3.3 Denatured Proteins as Self-Avoiding Random Coils, 82\u003c\/p\u003e \u003cp\u003e3.4 Modeling the Unfolded State, 82\u003c\/p\u003e \u003cp\u003e3.5 NN Effects in Protein Structure Prediction, 86\u003c\/p\u003e \u003cp\u003e3.6 Utilizing Folding Pathways for Structure Prediction, 87\u003c\/p\u003e \u003cp\u003e3.7 Native State Modeling, 88\u003c\/p\u003e \u003cp\u003e3.8 Secondary-Structure Propensities: Native Backbones in Unfolded Proteins, 92\u003c\/p\u003e \u003cp\u003e3.9 Conclusions, 92\u003c\/p\u003e \u003cp\u003eAcknowledgments, 93\u003c\/p\u003e \u003cp\u003eReferences, 94\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Short-Distance FRET Applied to the Polypeptide Chain 99\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMaik H. Jacob and Werner M. Nau\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 A Short Timeline of Resonance Energy Transfer Applied to the Polypeptide Chain, 99\u003c\/p\u003e \u003cp\u003e4.2 A Short Theory of FRET Applied to the Polypeptide Chain, 101\u003c\/p\u003e \u003cp\u003e4.3 DBO and Dbo, 105\u003c\/p\u003e \u003cp\u003e4.4 Short-Distance FRET Applied to the Structured Polypeptide Chain, 107\u003c\/p\u003e \u003cp\u003e4.5 Short-Distance FRET to Monitor Chain-Structural Transitions upon Phosphorylation, 116\u003c\/p\u003e \u003cp\u003e4.6 Short-Distance FRET Applied to the Structureless Chain, 120\u003c\/p\u003e \u003cp\u003e4.7 The Future of Short-Distance FRET, 125\u003c\/p\u003e \u003cp\u003eAcknowledgments, 125\u003c\/p\u003e \u003cp\u003eDedication, 126\u003c\/p\u003e \u003cp\u003eReferences, 126\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins 131\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eFranc Avbelj\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Local Structural Order in Unfolded Peptides and Proteins, 131\u003c\/p\u003e \u003cp\u003e5.2 ESM, 134\u003c\/p\u003e \u003cp\u003e5.3 The ESM and Strand-Coil Transition Model, 137\u003c\/p\u003e \u003cp\u003e5.4 The ESM and Backbone Conformational Preferences, 138\u003c\/p\u003e \u003cp\u003e5.5 The Nearest-Neighbor Effect, 141\u003c\/p\u003e \u003cp\u003e5.6 The ESM and Cooperative Local Structures—Fluctuating \u003ci\u003eβ\u003c\/i\u003e-Strands, 141\u003c\/p\u003e \u003cp\u003e5.7 The ESM and \u003ci\u003eβ\u003c\/i\u003e-Sheet Preferences in Native Proteins—Significance of Unfolded State, 144\u003c\/p\u003e \u003cp\u003e5.8 The ESM and Secondary Chemical Shifts of Polypeptides, 145\u003c\/p\u003e \u003cp\u003e5.9 Role of Backbone Solvation in Determining Hydrogen Exchange Rates of Unfolded Polypeptides, 148\u003c\/p\u003e \u003cp\u003e5.10 Other Theoretical Models of Unfolded Polypeptides, 148\u003c\/p\u003e \u003cp\u003eAcknowledgments, 149\u003c\/p\u003e \u003cp\u003eReferences, 149\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Experimental and Computational Studies of Polyproline II Propensity 159\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eW. Austin Elam, Travis P. Schrank, and Vincent J. Hilser\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction, 159\u003c\/p\u003e \u003cp\u003e6.2 Experimental Measurement of PII Propensities, 161\u003c\/p\u003e \u003cp\u003e6.3 Computational Studies of Denatured State Conformational Propensities, 168\u003c\/p\u003e \u003cp\u003e6.4 A Steric Model Reveals Common PII Propensity of the Peptide Backbone, 172\u003c\/p\u003e \u003cp\u003e6.5 Correlation of PII Propensity to Amino Acid Properties, 175\u003c\/p\u003e \u003cp\u003e6.6 Summary, 180\u003c\/p\u003e \u003cp\u003eAcknowledgments, 180\u003c\/p\u003e \u003cp\u003eReferences, 180\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Mapping Conformational Dynamics in Unfolded Polypeptide Chains Using Short Model Peptides by NMR Spectroscopy 187\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eDaniel Mathieu, Karin Rybka, Jürgen Graf, and Harald Schwalbe\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction, 187\u003c\/p\u003e \u003cp\u003e7.2 General Aspects of NMR Spectroscopy, 189\u003c\/p\u003e \u003cp\u003e7.3 NMR Parameters and Their Measurement, 191\u003c\/p\u003e \u003cp\u003e7.4 Translating NMR Parameters to Structural Information, 202\u003c\/p\u003e \u003cp\u003e7.5 Conclusions, 213\u003c\/p\u003e \u003cp\u003eAcknowledgments, 215\u003c\/p\u003e \u003cp\u003eReferences, 215\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Secondary Structure and Dynamics of a Family of Disordered Proteins 221\u003cbr\u003e \u003c\/b\u003e\u003ci\u003ePranesh Narayanaswami and Gary W. Daughdrill\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction, 221\u003c\/p\u003e \u003cp\u003e8.2 Materials and Methods, 223\u003c\/p\u003e \u003cp\u003e8.3 Results and Discussion, 226\u003c\/p\u003e \u003cp\u003eAcknowledgments, 235\u003c\/p\u003e \u003cp\u003eReferences, 235\u003c\/p\u003e \u003cp\u003e\u003cb\u003eII DISORDERED PEPTIDES AND MOLECULAR RECOGNITION 239\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Binding Promiscuity of Unfolded Peptides 241\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eChristopher J. Oldfi eld, Bin Xue, A. Keith Dunker, and Vladimir N. Uversky\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Protein–Protein Interaction Networks, 241\u003c\/p\u003e \u003cp\u003e9.2 Role of Intrinsic Disorder in PPI Networks, 242\u003c\/p\u003e \u003cp\u003e9.3 Transient Structural Elements in Protein-Based Recognition, 243\u003c\/p\u003e \u003cp\u003e9.4 Chameleons and Adaptors: Binding Promiscuity of Unfolded Peptides, 256\u003c\/p\u003e \u003cp\u003e9.5 Principles of Using the Unfolded Protein Regions for Binding, 262\u003c\/p\u003e \u003cp\u003e9.6 Conclusions, 266\u003c\/p\u003e \u003cp\u003eAcknowledgments, 266\u003c\/p\u003e \u003cp\u003eReferences, 266\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Intrinsic Flexibility of Nucleic Acid Chaperone Proteins from Pathogenic RNA Viruses 279\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRoland Ivanyi-Nagy, Zuzanna Makowska, and Jean-Luc Darlix\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction, 279\u003c\/p\u003e \u003cp\u003e10.2 Retroviruses and Retroviral Nucleocapsid Proteins, 280\u003c\/p\u003e \u003cp\u003e10.3 Core Proteins in the \u003ci\u003eFlaviviridae\u003c\/i\u003e Family of Viruses, 288\u003c\/p\u003e \u003cp\u003e10.4 Coronavirus Nucleocapsid Protein, 290\u003c\/p\u003e \u003cp\u003e10.5 Hantavirus Nucleocapsid Protein, 291\u003c\/p\u003e \u003cp\u003eAcknowledgments, 293\u003c\/p\u003e \u003cp\u003eReferences, 293\u003c\/p\u003e \u003cp\u003e\u003cb\u003eIII AGGREGATION OF DISORDERED PEPTIDES 307\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Self-Assembling Alanine-Rich Peptides of Biomedical and Biotechnological Relevance 309\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eThomas J. Measey and Reinhard Schweitzer-Stenner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Biomolecular Self-Assembly, 309\u003c\/p\u003e \u003cp\u003e11.2 Misfolding and Human Disease, 310\u003c\/p\u003e \u003cp\u003e11.3 Exploitation of Peptide Self-Assembly for Biotechnological Applications, 326\u003c\/p\u003e \u003cp\u003e11.4 Concluding Remarks, 340\u003c\/p\u003e \u003cp\u003eAcknowledgments, 340\u003c\/p\u003e \u003cp\u003eReferences, 340\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Structural Elements Regulating Interactions in the Early Stages of Fibrillogenesis: A Human Calcitonin Model System 351\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRosa Maria Vitale, Giuseppina Andreotti, Pietro Amodeo, and Andrea Motta\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Stating the Problem, 351\u003c\/p\u003e \u003cp\u003e12.2 Aggregation Models: The State of The Art, 354\u003c\/p\u003e \u003cp\u003e12.3 Human Calcitonin hCT as a Model System for Self-Assembly, 356\u003c\/p\u003e \u003cp\u003e12.4 The “Prefi brillar” State of hCT, 358\u003c\/p\u003e \u003cp\u003e12.5 How Many Molecules for the Critical Nucleus?, 361\u003c\/p\u003e \u003cp\u003e12.6 Modeling Prefi brillar Aggregates, 366\u003c\/p\u003e \u003cp\u003e12.7 hCT Helical Oligomers, 366\u003c\/p\u003e \u003cp\u003e12.8 The Role of Aromatic Residues in the Early Stages of Amyloid Formation, 372\u003c\/p\u003e \u003cp\u003e12.9 The Folding of hCT before Aggregation, 373\u003c\/p\u003e \u003cp\u003e12.10 Model Explains the Differences in Aggregation Properties between hCT and sCT, 374\u003c\/p\u003e \u003cp\u003e12.11 hCT Fibril Maturation, 375\u003c\/p\u003e \u003cp\u003e12.12 \u003ci\u003eα\u003c\/i\u003e-Helix →\u003ci\u003eβ\u003c\/i\u003e-Sheet Conformational Transition and hCT Fibrillation, 377\u003c\/p\u003e \u003cp\u003e12.13 Concluding Remarks, 378\u003c\/p\u003e \u003cp\u003eAcknowledgments, 378\u003c\/p\u003e \u003cp\u003eReferences, 379\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Solution NMR Studies of A\u003ci\u003eβ\u003c\/i\u003e Monomers and Oligomers 389\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eChunyu Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction, 389\u003c\/p\u003e \u003cp\u003e13.2 Overexpression and Purifi cation of Recombinant A\u003ci\u003eβ\u003c\/i\u003e, 390\u003c\/p\u003e \u003cp\u003e13.3 A\u003ci\u003eβ\u003c\/i\u003e Monomers, 393\u003c\/p\u003e \u003cp\u003e13.4 A\u003ci\u003eβ\u003c\/i\u003e Oligomers and Monomer–Oligomer Interaction, 403\u003c\/p\u003e \u003cp\u003e13.5 Conclusion, 406\u003c\/p\u003e \u003cp\u003eReferences, 406\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Thermodynamic and Kinetic Models for Aggregation of Intrinsically Disordered Proteins 413\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eScott L. Crick and Rohit V. Pappu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction, 413\u003c\/p\u003e \u003cp\u003e14.2 Thermodynamics of Protein Aggregation—the Phase Diagram Approach, 415\u003c\/p\u003e \u003cp\u003e14.3 Thermodynamics of IDP Aggregation (Phase Separation)—MPM Description, 420\u003c\/p\u003e \u003cp\u003e14.4 Kinetics of Homogeneous Nucleation and Elongation Using MPMs, 425\u003c\/p\u003e \u003cp\u003e14.5 Concepts from Colloidal Science, 427\u003c\/p\u003e \u003cp\u003e14.6 Conclusions, 433\u003c\/p\u003e \u003cp\u003eAcknowledgments, 433\u003c\/p\u003e \u003cp\u003eReferences, 434\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions 441\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMichal Levy-Sakin, Roni Scherzer-Attali, and Ehud Gazit\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction, 441\u003c\/p\u003e \u003cp\u003e15.2 Nonspecific Modifi ers, 442\u003c\/p\u003e \u003cp\u003e15.3 Specific Modifiers, 454\u003c\/p\u003e \u003cp\u003eAcknowledgments, 465\u003c\/p\u003e \u003cp\u003eReferences, 466\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Computational Studies of Folding and Assembly of Amyloidogenic Proteins 479\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJ. Srinivasa Rao, Brigita Urbanc, and Luis Cruz\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction, 479\u003c\/p\u003e \u003cp\u003e16.2 Amyloids, 480\u003c\/p\u003e \u003cp\u003e16.3 Computer Simulations, 485\u003c\/p\u003e \u003cp\u003e16.4 Summary, 514\u003c\/p\u003e \u003cp\u003eReferences, 515\u003c\/p\u003e \u003cp\u003e\u003cb\u003eINDEX 529\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eReinhard Schweitzer-Stenner, PhD,\u003c\/b\u003e 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.\u003c\/p\u003e  \u003cp\u003eSheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseases\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e \u003cp\u003eProtein 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:\u003c\/p\u003e \u003cul\u003e \u003cli\u003e \u003cp\u003eConformational Analysis of Unfolded States\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eDisordered Peptides and Molecular Recognition\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eAggregation of Disordered Peptides\u003c\/p\u003e \u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eThroughout 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.\u003c\/p\u003e \u003cp\u003eWith 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.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989879701733,"sku":"NP9780470591697","price":184.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9780470591697.jpg?v=1761785770","url":"https:\/\/k12savings.com\/es\/products\/protein-and-peptide-folding-misfolding-and-non-folding-isbn-9780470591697","provider":"K12savings","version":"1.0","type":"link"}