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Protein and peptide folding, misfolding, and non-folding [[electronic resource] /] / edited by Reinhard Schweitzer-Stenner
| Protein and peptide folding, misfolding, and non-folding [[electronic resource] /] / edited by Reinhard Schweitzer-Stenner |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2012 |
| Descrizione fisica | 1 online resource (596 p.) |
| Disciplina | 572/.633 |
| Altri autori (Persone) | Schweitzer-StennerReinhard |
| Collana | Wiley series in protein and peptide science |
| Soggetto topico |
Protein folding
Peptides |
| ISBN |
1-280-59177-3
9786613621603 1-118-18335-5 1-118-18337-1 1-118-18334-7 |
| Classificazione | SCI049000 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
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 DEPENDENT1.7. 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 AS1.14. 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 THEM2.2. 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 Aß-PEPTIDES; 2.8. CONCLUDING REMARKS; ACKNOWLEDGMENTS; REFERENCES 3: LOCAL BACKBONE PREFERENCES AND NEAREST-NEIGHBOR EFFECTS IN THE UNFOLDED AND NATIVE STATES Joe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick3.1. INTRODUCTION; 3.2. EARLY DAYS: RANDOM COIL-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 FORSTRUCTURE PREDICTION; 3.7. NATIVE STATE MODELING; 3.8. SECONDARY-STRUCTURE PROPENSITIES: NATIVE BACKBONES IN UNFOLDED PROTEINS; 3.9. CONCLUSIONS; ACKNOWLEDGMENTS; REFERENCES 4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau |
| Record Nr. | UNINA-9910141317703321 |
| Hoboken, N.J., : John Wiley & Sons, c2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein and peptide folding, misfolding, and non-folding / / edited by Reinhard Schweitzer-Stenner
| Protein and peptide folding, misfolding, and non-folding / / edited by Reinhard Schweitzer-Stenner |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2012 |
| Descrizione fisica | 1 online resource (596 p.) |
| Disciplina | 572/.633 |
| Altri autori (Persone) | Schweitzer-StennerReinhard |
| Collana | Wiley series in protein and peptide science |
| Soggetto topico |
Protein folding
Peptides |
| ISBN |
1-280-59177-3
9786613621603 1-118-18335-5 1-118-18337-1 1-118-18334-7 |
| Classificazione | SCI049000 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
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 DEPENDENT1.7. 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 AS1.14. 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 THEM2.2. 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 Aß-PEPTIDES; 2.8. CONCLUDING REMARKS; ACKNOWLEDGMENTS; REFERENCES 3: LOCAL BACKBONE PREFERENCES AND NEAREST-NEIGHBOR EFFECTS IN THE UNFOLDED AND NATIVE STATES Joe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick3.1. INTRODUCTION; 3.2. EARLY DAYS: RANDOM COIL-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 FORSTRUCTURE PREDICTION; 3.7. NATIVE STATE MODELING; 3.8. SECONDARY-STRUCTURE PROPENSITIES: NATIVE BACKBONES IN UNFOLDED PROTEINS; 3.9. CONCLUSIONS; ACKNOWLEDGMENTS; REFERENCES 4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau |
| Record Nr. | UNINA-9910814089803321 |
| Hoboken, N.J., : John Wiley & Sons, c2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||