1. National Taiwan Ocean UniversityDepartment of Bioscience and Biotechnology國立臺灣海洋大學生命科學暨生物科技學系
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2. Chapter 5Proteins: Their Primary Structure and Biological Function2015-10-15
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3. 5.5 What is the Nature of Amino Acid Sequences?
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4. 5.5 What is the Nature of Amino Acid Sequences?
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5. Homologous Proteins from Different Organisms Have Homologous Amino Acid Sequences
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6. Homologous proteins can be further subdivided into orthologous and paralogous proteins. Orthologous proteins are proteins from different species that have homologous amino acid sequences (and often a similar function). Orthologous proteins arose from a co
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7. Computer Programs Can Align Sequences and Discover Homology Between Proteins
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8. Blocks Substitution Matrix (BLOSUM)
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9. Computer Programs Can Align Sequences and Discover Homology Between Proteins
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10. Blocks Substitution Matrix (BLOSUM)
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11. Phylogeny of Cytochrome c
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12. Orthology in cytochrome c
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13. Related Proteins Show a Common Evolutionary Origin
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14. Related Proteins Show a Common Evolutionary Origin
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15. Slide 12
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16. Related Proteins Show a Common Evolutionary Origin
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17. Serine Proteases
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18. Apparently Different Proteins May Share a Common Ancestry
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19. Apparently Different Proteins May Share a Common Answer
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20. 5.7 Do Proteins Have Chemical Groups Other Than Amino Acids?
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21. 5.7 Do Proteins Have Chemical Groups Other Than Amino Acids?
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22. 5.8 What Are the Many Biological Functions of Proteins?
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23. 5.8 What Are the Many Biological Functions of Proteins?
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24. 5.8 What Are the Many Biological Functions of Proteins?
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25. 5.8 What Are the Many Biological Functions of Proteins?
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26. Chapter 6Proteins: Secondary, Tertiary, and Quaternary Structure
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27. Protein Structure and Function Are Tightly Linked
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28. Polypeptide Chains Are Flexible Yet Conformationally Restricted
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29. Slide 26
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30. Slide 27
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31. Slide 26
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32. Slide 27
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33. Slide 28
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34. Slide 29
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35. Slide 30
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36. Slide 29
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37. Slide 30
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38. Slide 31
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39. Slide 32
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40. Slide 33
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41. Secondary Structure: Polypeptide Chains Can Fold into Regular Structures Such As the Alpha Helix, the Beta Sheet, and Turns and Loops
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42. Steric Constraints on φ & ψ
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43. Secondary Structure: Polypeptide Chains Can Fold into Regular Structures Such As the Alpha Helix, the Beta Sheet, and Turns and Loops
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44. Slide 33
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45. Secondary Structure: Polypeptide Chains Can Fold into Regular Structures Such As the Alpha Helix, the Beta Sheet, and Turns and Loops
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46. Steric Constraints on φ & ψ
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47. Slide 36
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48. hydrogen-bonding capacity of the backbone NH and CO A tightly coiled backbone forms the inner part of the rod and the side chains extend outward in a helical array.In particular, the CO group of each amino acid forms a hydrogen bond with the NH group of t
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49. Slide 38
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50. The pitch of the α helix, which is equal to the product of the translation (1.5 A) and the number of residues per turn (3.6), is 5.4 A. The screw sense of a helixcan be right-handed (clockwise) or left -handed (counterclockwise).Essentially all α helices
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51. Slide 38
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52. The pitch of the α helix, which is equal to the product of the translation (1.5 A) and the number of residues per turn (3.6), is 5.4 A. The screw sense of a helixcan be right-handed (clockwise) or left -handed (counterclockwise).Essentially all α helices
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53. Slide 40
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54. Slide 41
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55. It is composed of two or more polypeptide chains called beta strands. A beta strand is almost fully extended rather than being tightly coiled as in the α helix. A range of extended structures are sterically allowed (Figure 2.34).
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56. Slide 43
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57. Slide 44
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58. Slide 45
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59. Slide 46
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60. Slide 47
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61. Most proteins have compact, globular shapes owing to reversals in the direction of their polypeptide chains. Many of these reversals are accomplished by a common structural element called the reverse turn (also knownas the beta turn or hairpin turn ), ill
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62. Amino Acids Have Different Propensities for Forming Alpha Helices, Beta Sheets, and Beta Turns
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63. Branching at the beta carbon atom, as in valine, threonine, and isoleucine, tends to destabilize alfa helices because of steric clashes, These residues are readily accommodated in beta strands, in which their side chains project out of the plane containin
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64. Slide 51
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65. Proline tends to disrupt both alfa helices and beta strands because it lacks an NH group and because its ring structure restricts its φ value to near 60 degrees. Glycine readily fits into all structuresand for that reason does not favor helix formation in
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66. These diseases include bovine spongiform encephalopathy (commonly referred to as mad cow disease) and the analogous diseases in other organisms, including Creutzfeldt–Jakob disease (vCJD or nvCJD), in human beings and scrapie in sheep.
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67. Slide 54
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68. Slide 55
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69. Slide 56
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70. Amyloid fibers are also seen in the brains of patients with certain noninfectious neurodegenerative diseases such as Alzheimer and Parkinson diseases.For example, the brains of patients with Alzheimer disease contain protein aggregates called amyloid plaq
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71. 6.1 What Noncovalent Interactions Stabilize the Higher Levels of Protein Structures?
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72. 6.1 What Noncovalent Interactions Stabilize the Higher Levels of Protein Structure?
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73. Electrostatic Interactions in Proteins
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74. Electrostatic Interactions in Proteins
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75. 6.2 What Role Does the Amino Acid Sequence Play in Protein Structure?
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76. 6.4 How Do Polypeptides Fold into Three-Dimensional Protein Structures?
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77. Waters on the Protein Surface Stabilize the Structure
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78. Waters on the Protein Surface Stabilize the Structure
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79. Protein domains are nature’s modular strategy for protein design
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80. Most domains consist of a single continuous portion of the protein sequence
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81. A large domain consisting of two sequences interrupted by the sequence of another domain
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82. Most domains consist of a single continuous portion of the protein sequence
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83. Protein domains are nature’s modular strategy for protein design
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84. Most domains consist of a single continuous portion of the protein sequence
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85. A large domain consisting of two sequences interrupted by the sequence of another domain
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86. Many proteins are composed of several distinct domains
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87. Many proteins are composed of several distinct domains
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88. Denaturation Leads to Loss of Protein Structure and Function
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89. Denaturation Leads to Loss of Protein Structure and Function
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90. Most Globular Proteins Belong to One of Four Structural Classes
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91. Most Globular Proteins Belong to One of Four Structural Classes
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92. Molecular Chaperones Are Proteins That Help Other Proteins to Fold
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93. α1-Antitrypsin – A Tale of Molecular Mousetraps and a Folding Disease
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94. α1-Antitrypsin – A Tale of Molecular Mousetraps and a Folding Disease
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95. 6.5 How Do Protein Subunits Interact at the Quaternary Level of Structure?
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96. α1-Antitrypsin – A Tale of Molecular Mousetraps and a Folding Disease
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97. α1-Antitrypsin – A Tale of Molecular Mousetraps and a Folding Disease
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98. Molecular Chaperones Are Proteins That Help Other Proteins to Fold
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99. Most Globular Proteins Belong to One of Four Structural Classes
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100. Most Globular Proteins Belong to One of Four Structural Classes
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101. Denaturation Leads to Loss of Protein Structure and Function
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102. Denaturation Leads to Loss of Protein Structure and Function
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103. Many proteins are composed of several distinct domains
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104. Denaturation Leads to Loss of Protein Structure and Function