Hierarchical protein folding: Asymmetric unfolding of an insulin analogue lacking the A7-B7 interchain disulfide bridge

Biochemistry

Volumn 40, Issue 41, 2001, Pages 12299-12311

  Hua, Q X ^a   Nakagawa, S H ^b   Jia, W ^a   Hu, S Q ^c   Chu, Y C ^c   Katsoyannis, P G ^c   Weiss, M A ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

^c NEW YORK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN FOLDING;

BIOCHEMISTRY; MOLECULES; THERMODYNAMIC STABILITY;

PROTEINS;

CYSTINE; DISULFIDE; INSULIN DERIVATIVE; MONOMER; PROINSULIN; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL BOND; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE;

CIRCULAR DICHROISM; DISULFIDES; DRUG STABILITY; HUMANS; INSULIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROINSULIN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; THERMODYNAMICS;

EID: 0035899983     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi011021o     Document Type: Article

References (94)

1. An overview of insulin evolution
2. The role of assembly in insulin's biosynthesis
3. The structure of 2Zn pig insulin crystals at 1.5 Å resolution
4. Insulin synthesis by recombination of A and B chains: A highly efficient method
5. Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11, A6-B7-cystine] and [A6-A7, A11-B7-cystine] insulin (human)
6. The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide isomerase
7. Disulfide exchange folding of insulin-like growth factor I
8. Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: A bifurcating protein-folding pathway
9. Folding of insulin-like growth factor I is thermodynamically controlled by insulin-like growth factor binding protein
10. Putative folding pathway of insulin-like growth factor-I
11. Disulfide exchange folding of disulfide mutants of insulin like growth factor I in vitro
12. Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)-IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry
13. Intra-A chain disulphide bond forms first during insulin precursor folding
14. Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro
15. Studies on the total synthesis of an A7,B7-dicarbainsulin. III. Assembly of segments and generation of biological activity
16. Probing the disulfide folding pathway of insulin-like growth factor-I
17. Evidence for a precursor in the biosynthesis of insulin
18. Single chain des-(B30) insulin. Intramolecular crosslinking of insulin by trypsin catalyzed transpeptidation
19. Altering the association properties of insulin by amino acid replacement
20. Secretory expression of a single-chain insulin precursor in yeast and its conversion into human insulin
21. (A-C-B) human proinsulin, a novel insulin agonist and intermediate in the synthesis of biosynthetic human insulin
22. Steric requirements at position B 12 for high biological activity in insulin
23. A peptide model of a protein folding intermediate
24. Is protein folding hierarchic? II. Folding intermediates and transition states
25. A kinetic explanation for the rearrangement pathway of BPTI folding
26. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates
27. Conformations of intermediates in the folding of the pancreatic trypsin inhibitor
28. 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor
29. Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond
30. 13C labeling with application to protein design
31. Mutations at the dimer, hexamer, and receptor-binding, surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions
32. Mapping the functional surface of insulin by design: Structure and function of a novel A-chain analogue
33. Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: Genetic models of protein-folding intermediates
34. B24] insulin mutants: A steady-state fluorescence anisotrophy study
35. Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition
36. Receptor binding redefined by a structural switch in a mutant human insulin
37. Application of circular dichroism to study RNA folding transitions
38. Linear extrapolation method of analyzing solvent denaturation curves
39. How Ala→Gly mutations in different helices affect the stability of the apomyoglobin molten globule
40. Hierarchiacal protein "undesign": Insulin's intrachain disulfide bridge tethers a recognition α-helix
41. Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: Interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model
42. 1H NMR with application to phage lambda repressor
43. Native and non-native structure in a protein-folding intermediate: Spectroscopic studies of partially reduced IGF-I and an engineered alanine model
44. Native and non-native intermediates in the BPTI folding pathway
45. Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of its native and molten globule states
46. Structural characterization of the disulfide folding intermediates of bovine α-lactalbumin
47. Does the molten globule have a native-like tertiary fold?
48. Following protein folding in real time using NMR spectroscopy
49. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds
50. Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways
51. Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond
52. Two new structured intermediates in the oxidative folding of RNase A
53. Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: Further insights into the folding process
54. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
55. Hydrophobicity regained
56. Effects of cysteine to serine substitutions in the two intra-A-chain disulfide bonds of insulin
57. Receptor-binding region of insulin
58. Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin
59. A proposed interaction model of the insulin molecule with its receptor
60. Structure of insulin in 4-zinc insulin
61. Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer
62. Spectroscopic signatures of the T to R conformational transition in the insulin hexamer
63. Insulin hexamers: New conformations and applications
64. The structural basis of insulin and insulin-like growth factor-I receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signalling
65. Mutations at positions 11 and 60 of insulin-like growth factor 1 reveal differences between its interactions with the type I insulin-like-growth-factor receptor and the insulin receptor
66. Engineering the C-region of human insulin-like growth factor-1: Implications for receptor binding
67. Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: Implications for receptor binding
68. Structure of a protein in a kinetic trap
69. Three-dimensional solution structure of a disulfide bond isomer of the human insulin-like growth factor-I
70. Roles of disulfide bonds in recombinant human interleukin 6 conformation
71. An amino acid code for protein folding
72. "New view" of protein folding reconciled with the old through multiple unfolding simulations
73. The nature of protein folding pathways: The classical versus the new view
74. Theory of protein folding: The energy landscape perspective
75. Pathways for protein folding: Is a new view needed?
76. Solution structure of an engineered insulin monomer at neutral pH
77. Structure function studies with derivatives and analogs of insulin and its chains
78. Selective cleavage of one disulfide bond in insulin: Preparation and properties of insulin A7-B7-di-S-sulfonate
79. Synthesis and biological activity of seventeen analogues of human insulin
80. Characteristic, activity and conformational studies of [A6-Ser, A11-Ser]-insulin
81. Reexamination of the folding of BPTI: Predominance of native intermediates
82. From Levinthal to pathways to funnels
83. A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor
84. Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor. Forming the first disulphide bonds in analogues of the reduced protein
85. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor
86. Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor
87. Dynamics of the conformational ensemble of partially folded bovine pancreatic trypsin inhibitor
88. Structural effects induced by removal of a disulfide-bridge: The X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 Å
89. 15N relaxation measurements
90. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor
91. The roles of partly folded intermediates in protein folding