Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix

Journal of Molecular Biology

Volumn 296, Issue 4, 2000, Pages 1039-1051

  Forge, Vincent ^a   Hoshino, Masaru ^a   Kuwata, Kazuo ^b   Arai, Munehito ^c   Kuwajima, Kunihiro ^c   Batt, Carl A ^d   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b GIFU UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d Department of Obstetrics Gynecology   (United States)

Author keywords

Hydrogen deuterium exchange; Intermediate state; NMR; Protein folding; lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN;

ALPHA HELIX; ARTICLE; HYDROPHOBICITY; KINETICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; REACTION ANALYSIS; STRUCTURE ANALYSIS;

EID: 0034598947     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3515     Document Type: Article

References (57)

1. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
2. Primary structure effects on peptide group hydrogen exchange
3. Following protein folding in real time using NMR spectroscopy
4. Is protein folding hierarchic? I. Local structure and peptide folding
5. Is protein folding hierarchic? II. Folding intermediates and transition states
6. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
7. Bovine β-lactoglobulin at 1.8 Å resolution: Still an enigmatic lipocalin
8. Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
9. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
10. Isotope effects in peptide group hydrogen exchange
11. A tale of two secondary structure elements: When a β-hairpin becomes an α-helix
12. Transmuting α-helices and β-sheets
13. NMRPipe: A multidimensional spectral processing system based on UNIX Pipes
14. Protein folding: A perspective from theory and experiment
15. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
16. Theoretical studies of protein folding
17. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
18. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
19. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
20. β-Lactoglobulin
21. Evidence for an obligatory intermediate in the folding of interleukin 1-β
22. The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
23. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
24. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
25. β-Lactoglobulin B: A proposed standard for the study reversible self-associations in the analytical ultracentrifuge?
26. Trifluoroethanol promotes helix formation by destabilizing backbone exposure: Desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding
27. Kinetic traps in lysozyme folding
28. Intermediates in the folding reactions of small proteins
29. High level expression of bovine β-lactoglobulin in Pichia pastoris and characterization of its physical properties
30. Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization
31. MOL-MOL: A program for display and analysis of macro-molecular structures
32. High helical propensity of the peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy
33. Stopped-flow circular dichroism
34. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
35. α → β transition of β-lactoglobulin as evidenced by heteronuclear NMR
36. Solution structure and dynamics of bovine β-lactoglobulin A
37. A simple method for displaying the hydrophobic character of a protein
38. Structure of the transition state for folding of the 129 aa protein Che Y resembles that of a smaller protein, CI-2
39. Acceleration of the folding of hen lysozyme by trifluoroethanol
40. Does trifluoroethanol affect folding pathways and can it be used as a probe of structure in transition states?
41. Folding pathways of FKBP12 and characterization of the transition state
42. Detection of transient protein folding populations by mass spectrometry
43. Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme
44. Structural basis of latency in plasminogen activator inhibitor-1
45. Predicting protein secondary structure based on amino acid sequence
46. Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain
47. Prion diseases and the BSE crisis
48. Molten globule and protein folding
49. Structural basis of the Tanford transition of bovine β-lactoglobulin
50. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2
51. Kinetic role of early intermediates in protein folding
52. Prolyl isomerase: Enzyme catalysis of slow protein-folding reactions
53. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
54. Evidence for barrier-limited protein folding kinetics on the micro-second time scale
55. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
56. LINUS: A hierarchic procedure to predict the fold of a protein
57. Kinetics of folding of the all-β sheet protein interleukin-1β