Characterization of pH-induced transitions of β-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies

Journal of Molecular Biology

Volumn 314, Issue 4, 2001, Pages 873-889

  Taulier, Nicolas ^a   Chalikian, Tigran V ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Compressibility; Conformational transitions; Hydration; Volume; lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN;

ARTICLE; COMPRESSION; CONFORMATIONAL TRANSITION; HYDRATION; MOLECULAR DYNAMICS; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; X RAY CRYSTALLOGRAPHY;

EID: 0035824880     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5188     Document Type: Article

References (83)

1. Nomenclature of proteins of cow's milk: Fifth revision
2. Solution structure and dynamics of bovine β-lactoglobulin A
3. New insight into the pH-dependent conformational changes in bovine β-lactoglobulin from Raman optical activity
4. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
5. Pressure denaturation of β-lactoglobulin
6. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin
7. Molecular interactions in β-lactoglobulin. V. The association of the genetic species of β-lactoglobulin below the isoelectric point
8. 1. Structural differences between genetic variants A and B and features of the Tanford transition
9. Structural basis of the Tanford transition of bovine β-lactoglobulin
10. Bovine β-lactoglobulin at 1.8 Å resolution - Still an enigmatic lipocalin
11. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2
12. Effect of pH on β-lactoglobulins
13. Ultracentrifugal and electrophoretic studies on the milk proteins. II. The lactoglobulins of Palmer
14. Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of self-associating globular protein
15. Structure of the β-lactoglobulin tetramer
16. Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
17. Conformational transitions of bovine β-lactoglobulins A, B, and C
18. The reversible transformation of β-lactoglobulin at pH 7.5
19. Effect of pH on the denaturation of beta-lactoglobulin and its dodecyl sulfate derivative
20. Alkaline denaturation of β-lactoglobulins. Activation parameters and effect of dye binding site
21. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review
22. Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix
23. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
24. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
25. Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin
26. Adiabatic compressibility of myoglobin. Effects of axial ligand and denaturation
27. Specific volumes of biological macromolecules and some other molecules of biological interest
28. Amino acid, peptide, and protein volume in solution
29. Protein structure and dynamics at high pressure
30. Hydration and partial compressibility of biological compounds
31. Thermodynamic analysis of biomolecules: A volumetric approach
32. Volumetric properties of nucleic acids
33. Volumetric characterizations of the native, molten, and unfolded states of cytochrome c at acidic pH
34. Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: Characterization of the base-induced unfolded state at 25°C
35. The native and the heat-induced denatured states of α-chymotrypsinogen A: Thermodynamic and spectroscopic studies
36. Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease
37. Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
38. Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior
39. Adiabatic compressibility of molten globules
40. Hydration and protein folding in water and in reverse micelles. Compressibility and volume changes
41. Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B
42. Effect of pH on the structure and aggregation of human glycodelin A. A comparison with β-lactoglobulin
43. Estimation of globular protein secondary structure from circular dichroism
44. Hydration of proteins and polypepdites
45. Compressibility-structure relationship of globular proteins
46. The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamics and structural data
47. Protein denaturation. Parts A and B
48. Protein denaturation. Part C
49. Three-state analysis of sperm whale apomyoglobin folding
50. Volume changes of the molten globule transition of horse heart ferricytochrome c: A thermodynamic cycle
51. Slow folding kinetics of ribonuclease A by volume change and circular dichroism: Evidence for two independent reactions
52. as in proteins
53. as of ionizable groups in proteins
54. a's of ionizable residues in proteins: Semi-microscopic and microscopic aproaches
55. a calculations: Conformational averaging versus the average structure
56. Hydration of diglycyl tripepdides with nonpolar side-chains: A volumetric study
57. Relative sound velocities of sea salts at 25°C
58. Relaxational contributions to protein compressibility from ultrasonic data
59. Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5
60. Molecular interactions in β-lactoglobulin. VI. The dissociation of the genetic species of β-lactoglobulin at acid pH's
61. Pressure stability of proteins
62. Hydrostatic and osmotic pressure as tools to study macromolecular recognition
63. On volume changes accompanying conformational transitions of biopolymers
64. Compressibility as a means top detect and characterize globular protein states
65. Ionization-linked changes in protein conformation. II. The N → R transition in β-lactoglobulin
66. The interpretation of protein structures: Estimation of static accessibility
67. Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point
68. Density and volume change measurements
69. Ultrasonic measurements with millilitre liquid samples in the 0.5-100 MHz range
70. Development of methods of precise ultrasonic measurements in small volumes of liquids
71. Ultrasonic velocity and attenuation measurements in liquids with resonator, extending the MHz frequency range
72. Broad-band ultrasonic measurement techniques for liquids
73. Constant-path acoustic interferometer with transition layers for precision measurements in small liquid volumes
74. Theoretical analysis of an ultrasonic interferometer for precise measurements at high pressures
75. The velocity of sound in electrolytic solutions
76. Standard partial molal compressibilities by ultrasonics. 1. Sodium chloride and potassium chloride at 25°C
77. The Protein Data Bank: A computer-based archival file for macromolecular structure
78. Areas, volumes, packing and protein structure
79. The volume of atoms on the protein surface: Calculated from simulation, using Voronoi polyhedra
80. Volume changes on protein folding
81. A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites