Pressure effect on denaturant-induced unfolding of hen egg white lysozyme

Proteins: Structure, Function and Genetics

Volumn 44, Issue 3, 2001, Pages 180-187

  Sasahara, Kenji ^a,b   Sakurai, Masao ^a,c   Nitta, Katsutoshi ^b,c  

^a HOKKAIDO UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Cooperativity; Hydrostatic pressure; Intermediate state; Protein unfolding; Stability

Indexed keywords

EGG WHITE; LYSOZYME;

ARTICLE; CONFORMATIONAL TRANSITION; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE SENSITIVITY; THERMODYNAMICS; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CHICKENS; COMPUTATIONAL BIOLOGY; DOSE-RESPONSE RELATIONSHIP, DRUG; EGG PROTEINS; GUANIDINE; MURAMIDASE; PRESSURE; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0035882536     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1083     Document Type: Article

References (64)

1. Thermodynamics of structural stability and cooperative folding behavior in proteins
2. Collapse and cooperativity in protein folding
3. Stability of proteins
4. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
5. Thermodynamic properties of an extremely rapid protein folding reaction
6. Folding kinetics of a fluorescent variant of monomeric λ repressor
7. How do small single-domain protein fold?
8. Molten globule and protein folding
9. Role of the molten globule state in protein folding
10. Understanding how proteins fold: The lysozyme story so far
11. The crystal structure of lysozyme by X-ray diffraction
12. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride 2. Dependence on denaturant concentration at 25°
13. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
14. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
15. The folding of hen lysozyme involves partially structured intermediates and multiple pathways
16. Kinetic traps in lysozyme folding
17. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
18. Understanding protein folding via free-energy surfaces from theory and experiment
19. Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
20. Pressure effects on enzyme activity and stability at high temperatures
21. High pressure effects on protein structure and function
22. Protein structure and dynamics at high pressure
23. 1H NMR
24. Pressure-induced changes in the folded structure of lysozyme
25. Pressure stability of proteins
26. Thermodynamics of unfolding
27. Thermodynamics of protein denaturation: Effect of pressure on the denaturation of ribonuclease A
28. Reversible pressure-temperature denaturation of chymotrypsinogen
29. Pressure denaturation of metmyoglobin
30. Highresolution NMR study of the pressure-induced unfolding of lysozyme
31. The catalytic activities of monomeric enzymes show complex pressure dependence
32. Pressure effects on protein flexibility monomeric proteins
33. The preparation of guanidine hydrochloride
34. Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution
35. Determination and analysis of urea and guanidine hydrochloride denaturation curves
36. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
37. Partially unfolded equilibrium state of hen lysozyme studied by circular dichroism spectroscopy
38. A lysozyme folding intermediate revealed by solution X-ray scattering
39. Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme
40. On volume changes accompanying conformational transitions of biopolymers
41. Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
42. On the nature of protein interior
43. Some factors in the interpretation of protein denaturation
44. Volume effects in aqueous solutions of macromolecules containing non-polar groups
45. Hydrophobicity of amino acid residues in globular proteins
46. Effect of hydrostatic pressure on unfolding of α-lactalbumin: Volumetric equivalence of the molten globule and unfolded state
47. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
48. Heat capacity and conformation of proteins in the denatured state
49. Hydration of denatured and molten globule proteins
50. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
51. Protein interactions with urea and guanidine chloride
52. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
53. Water penetration and escape in proteins
54. 1H NMR spectroscopy
55. NMR study of the cold, heat, and pressure unfolding of ribonuclease A
56. Protein folding in the absence of chemical denaturants
57. Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior
58. Glycerol decreases the volume and compressibility of protein interior
59. Arc repressor will not denature under pressure in the absence of water
60. Protein destabilization at low temperatures
61. Cold denaturation and heat denaturation of streptomyces subtilisin inhibitor
62. Heat and cold denaturation of phosphoglycerate kinase (interaction of domains)
63. Solution X-ray scattering analysis of cold- heat-, and ureadenatured states in a protein, streptomyces subtilisin inhibitor
64. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates