Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin

International Dairy Journal

Volumn 12, Issue 4, 2002, Pages 319-329

  Jameson, Geoffrey B ^a   Adams, Julian J ^a   Creamer, Lawrence K ^b  

^a Institute of Fundamental Sciences   (New Zealand)

^b NEW ZEALAND DAIRY RESEARCH INSTITUTE   (New Zealand)

Author keywords

Lactoglobulin; Entropic stabilization; Flexible loops; Hydrophobic pocket; Nuclear magnetic resonance; Structure; X ray crystallography

Indexed keywords

BOVINAE;

EID: 0036228989     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(02)00028-6     Document Type: Article

References (50)

1. Structure of porcine beta-lactoglobulin
2. A theoretical approach to possible biological functions of the milk-whey proteins, α-lactalbumin and β-lactoglobulin
3. Crystal forms of β-lactoglobulin
4. New stable folding of β-lactoglobulin induced by 2-propanol
5. Thermal denaturation of β-lactoglobulin
6. The protein data bank
7. Bovine β-lactoglobulin and its variants: A three-dimensional structural perspective
8. Bovine β-lactoglobulin at 1.8Å, resolution - Still an enigmatic lipocalin
9. Crystallography & NMR system: A new software suite for macromolecular structure determination
10. Relationship between milk protein polymorphism and physico-chemical properties
11. Alcohol-induced changes of β-lactoglobulin - Retinol-binding stoichiometry
12. Heat-resistant structural features of bovine β-lactoglobulin A revealed by NMR H/D exchange measurements
13. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
14. The relationship between milk protein polymorphism and the manufacture and functionality of dairy products
15. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2
16. The 'dynbamics' in the thermodynamics of binding
17. Interactions between β-lactoglobulin and flavour compounds
18. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
19. β-Lactoglobulin
20. Effect of the bovine β-lactoglobulin phenotype on the properties of β-lactoglobulin, milk composition, and dairy products
21. Alcohol-induced denaturation of β-lactoglobulin: A close correlation to the alcohol-induced α-helix formation of melittin
22. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
23. Solution structure and dynamics of bovine β-lactoglobulin A
24. PROCHECK: A program to check the stereochemical quality of protein structure
25. AmoRe: An automated package for molecular replacement
26. Protein folding and association: Insights from the interracial and thermodynamic properties of hydrocarbons
27. Retinoid-binding proteins: Mediators of retinoid action
28. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin
29. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review
30. Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk
31. Structural basis of the Tanford transition of bovine β-lactoglobulin
32. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin
33. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
34. Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements
35. Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach
36. Milk proteins: Structure and biological functions
37. The core lipocalin, bovine β-lactoglobulin
38. Milk protein structure - What can it tell the dairy industry?
39. Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
40. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierachial protein folding
41. Effect of increased loop flexibility on the structure and stability of a de novo designed helical protein
42. NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
43. Molecular surface area and hydrophobic effect
44. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
45. Structures and functionalities of milk proteins
46. β-Lactoglobulin binds palmitate within its central cavity
47. Increased protein backbone conformational entropy upon hydrophobic ligand binding