LEADER 05480nam 2200697Ia 450 001 9910814089803321 005 20240514070258.0 010 $a1-280-59177-3 010 $a9786613621603 010 $a1-118-18335-5 010 $a1-118-18337-1 010 $a1-118-18334-7 035 $a(CKB)2670000000148272 035 $a(EBL)818526 035 $a(OCoLC)777374858 035 $a(SSID)ssj0000622312 035 $a(PQKBManifestationID)11392465 035 $a(PQKBTitleCode)TC0000622312 035 $a(PQKBWorkID)10637284 035 $a(PQKB)10351106 035 $a(MiAaPQ)EBC818526 035 $a(Au-PeEL)EBL818526 035 $a(CaPaEBR)ebr10533977 035 $a(CaONFJC)MIL362160 035 $a(EXLCZ)992670000000148272 100 $a20111031d2012 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aProtein and peptide folding, misfolding, and non-folding /$fedited by Reinhard Schweitzer-Stenner 205 $a1st ed. 210 $aHoboken, N.J. $cJohn Wiley & Sons$dc2012 215 $a1 online resource (596 p.) 225 1 $aWiley series in protein and peptide science ;$v13 300 $aDescription based upon print version of record. 311 $a0-470-59169-2 320 $aIncludes bibliographical references and index. 327 $aPROTEIN 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 327 $a1.6. 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 327 $a1.13. 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 327 $a2.1. 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 327 $a3: 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 327 $a4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau 330 $aSheds new light on intrinsically disordered proteins and peptides, including their role in neurodegenerative diseases With the discovery of intrinsically disordered proteins and peptides (IDPs), researchers realized that proteins do not necessarily adopt a well defined secondary and tertiary structure in order to perform biological functions. In fact, IDPs play biologically relevant roles, acting as inhibitors, scavengers, and even facilitating DNA/RNA-protein interactions. Due to their propensity for self-aggregation and fibril formation, some IDPs are involved in neurodegenerative dis 410 0$aWiley series in protein and peptide science ;$v13. 606 $aProtein folding 606 $aPeptides 615 0$aProtein folding. 615 0$aPeptides. 676 $a572/.633 686 $aSCI049000$2bisacsh 701 $aSchweitzer-Stenner$b Reinhard$01717956 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910814089803321 996 $aProtein and peptide folding, misfolding, and non-folding$94114602 997 $aUNINA