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Peptide Folding, Misfolding, and Nonfolding.
Sheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseasesWith the discovery of intrinsically disordered proteins and peptides (IDPs), researchers realized that proteins do not necessarily adopt a well defined secondary and tertiary structur...
| Clasificación: | Libro Electrónico |
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| Autor principal: | |
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Hoboken :
John Wiley & Sons,
2012.
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| Temas: | |
| Acceso en línea: | Texto completo |
MARC
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| 100 | 1 | |a Schweitzer-Stenner, Reinhard. | |
| 245 | 1 | 0 | |a Peptide Folding, Misfolding, and Nonfolding. |
| 260 | |a Hoboken : |b John Wiley & Sons, |c 2012. | ||
| 300 | |a 1 online resource (596 pages) | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
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| 505 | 0 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 500 | |a 4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau. | ||
| 520 | |a Sheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseasesWith 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. | ||
| 588 | 0 | |a Print version record. | |
| 590 | |a ProQuest Ebook Central |b Ebook Central Academic Complete | ||
| 650 | 0 | |a Peptides. | |
| 650 | 0 | |a Protein folding. | |
| 650 | 6 | |a Peptides. | |
| 650 | 6 | |a Protéines |x Repliement. | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a NATURE |x Animals |x Mammals. |2 bisacsh | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Zoology |x Mammals. |2 bisacsh | |
| 650 | 7 | |a Peptides |2 fast | |
| 650 | 7 | |a Protein folding |2 fast | |
| 700 | 1 | |a Uversky, Vladimir N. | |
| 758 | |i has work: |a Peptide Folding, Misfolding, and Nonfolding [electronic resource] (Text) |1 https://id.oclc.org/worldcat/entity/E39PCYVgWmgv9TjJ8FmwxXXVKH |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |a Schweitzer-Stenner, Reinhard. |t Peptide Folding, Misfolding, and Nonfolding. |d Hoboken : John Wiley & Sons, ©2012 |z 9780470591697 |
| 856 | 4 | 0 | |u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=818526 |z Texto completo |
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