Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions

Proteins: Structure, Function and Genetics

Volumn 49, Issue 4, 2002, Pages 472-482

  Sasahara, Kenji ^a,b,c   Demura, Makoto ^a   Nitta, Katsutoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Folding intermediate; Hen egg white lysozyme; Protein folding; Stopped flow

Indexed keywords

ALPHA LACTALBUMIN; EGG WHITE; GUANIDINE; LYSOZYME;

ARTICLE; CHICKEN; CIRCULAR DICHROISM; EGG; KINETICS; MOLECULAR INTERACTION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS;

ACIDS; ANIMALS; CHICKENS; CIRCULAR DICHROISM; FEMALE; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; LACTALBUMIN; MODELS, CHEMICAL; MURAMIDASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; TEMPERATURE; THERMODYNAMICS;

EID: 0036892357     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10215     Document Type: Article

References (55)

1. Kim PS, Baldwin RL. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 1990;59:631-660.
2. Arai M, Kuwajima K. Role of the molten globule state in protein folding. Adv Protein Chem 2000;53:209-282.
3. Chamberlain AK, Marqusee S. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Adv Protein Chem 2000;53:283-328.
4. Ptitsyn OB. Molten globule and protein folding. Adv Protein Chem 1995;47:83-229.
5. Jackson SE. How do small single-domain protein fold? Fold Design 1998;3:R81-R91.
6. Dill KA, Chan HS. From levinthal to pathways to funnels. Nat Struct Biol 1997;4:10-19.
7. Shakhnovich EI. Theoretical studies of protein folding thermodynamics and kinetics. Curr Opin Struct Biol 1997;7:29-40.
8. Creighton TE. The energetic ups and downs of protein folding. Nat Struct Biol 1994;1:135-138.
9. Baldwin RL. On-pathway versus off-pathway folding intermediates. Fold Design 1996;1:R1-R8.
10. Roder H, Colon W. Kinetic role of early intermediates in protein folding. Curr Opin Struct Biol 1997;7:15-28.
11. Tanford C, Aune KC, Ikai A. Kinetics of unfolding and refolding of proteins. 3. Results for lysozyme. J Mol Biol 1973;73:185-197.
12. Kato S, Okamura M, Shimamoto N, Utiyama H. Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme. Biochemistry 1981;20:1080-1085.
13. Kuwajima K, Hiraoka Y, Ikeguchi M, Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 1985;24:874-881.
14. Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 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. Biochemistry 1986;25:6965-6972.
15. Chaffotte AF, Guillou Y, Goldberg ME. Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry 1992;31:9694-9702.
16. Miranker A, Radford SE, Karplus M, Dobson CM. Demonstration by NMR of folding domains in lysozyme. Nature 1991;349:633-636.
17. Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM. Detection of transient protein folding populations by mass spectrometry. Science 1993;262:896-900.
18. Radford SE, Dobson CM, Evans PA. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 1992;358:302-307.
19. 127)-lysozyme: A stopped-flow absorbance and fluorescence study. Biochemistry 1994;33:11225-11236.
20. Itzhaki LS, Evans, PA, Dobson CM, Radford SE. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 1994;33:5212-5220.
21. Matagne A, Radford SE, Dobson CM. Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process. J Mol Biol 1997;267:1068-1074.
22. Matagne A, Chung EW, Ball LJ, Radford SE, Robinson CV, Dobson CM. The origin of the α-domain intermediate in the folding of hen lysozyme. J Mol Biol 1998;277:997-1005.
23. Kiefhaber T. Kinetic traps in lysozyme folding. Proc Natl Acad Sci USA 1995;92:9029-9033.
24. Gladwin ST, Evans PA. Structure of very early protein folding intermediates: New insight through a variant of hydrogen exchange labeling. Fold Design 1996;1:407-417.
25. Rothwarf DM, Scheraga HA. Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry 1996;35:13797-13807.
26. Wildegger G, Kiefhaber T. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate. J Mol Biol 1997;270:294-304.
27. Segel DJ, Bachmann A, Hofrichter J, Hodgson KO, Doniach S, Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle x-ray scattering. J Mol Biol 1999;288:489-499.
28. Bai Y. Kinetic evidence of an on-pathway intermediate in the folding of lysozyme. Protein Sci 2000;9:194-196.
29. Sasahara K, Demura M, Nitta K. Partially unfolded equilibrium state of hen lysozyme studied by circular dichroism spectroscopy. Biochemistry 2000;39:6475-6482.
30. Sasahara K, Sakurai M, Nitta K. Pressure effect on denaturant-induced unfolding of hen egg white lysozyme. Proteins 2001;44:180-187.
31. Chen L, Wildegger G, Kiefhaber T, Hodgson KO, Doniach S. Kinetics of lysozyme refolding: Structural characterization of a non-specifically collapsed state using time-resolved x-ray scattering. J Mol Biol 1998;276:225-237.
32. Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol 1972;26:43-50.
33. Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 1986;131:266-280.
34. Santoro MM, Bolen DW. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl a-chymotrypsin using different denaturants. Biochemistry 1988;27:8063-8068.
35. Arai M, Kuwajima K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold Design 1996;1:275-287.
36. Khorasanizadeh S, Peters ID, Roder H. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat Struct Biol 1996;3:193-205.
37. Matouschek A, Kellis JT Jr, Serrano L, Bycroft M, Fersht AR. Transient folding intermediates characterized by protein engineering. Nature 1990;346:440-445.
38. Mizuguchi M, Arai M, Ke Y, Nitta K, Kuwajima K. Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy. J Mol Biol 1998;283:265-277.
39. Matagne A, Dobson CM. The folding process of hen lysozyme: A perspective from the "new view." Cell Mol Life Sci 1998;54:363-371.
40. Mckenzie HA, White FH Jr. Lysozyme and α-lactalbumin: Structure, function, and interrelationship. Adv Protein Chem 1991;41:173-315.
41. Nitta K, Sugai S. The evolution of lysozyme and α-lactalbumin. Eur J Biochem 1989;182:111-118.
42. Haezebrouck P, Noyelle K, Van Dael H. Equilibrium and kinetic folding of pigeon lysozyme. Biochemistry 1998;37:6772-6780.
43. Gast K, Zirwer D, Muller-Frohne M, Damaschun G. Compactness of the kinetic molten globule of bovine alpha-lactalbumin: A dynamic light scattering study. Protein Sci 1998;7:2004-2011.
44. Hooke SD, Radford SE, Dobson CM. The refolding of human lysozyme: A comparison with the structurally homologous hen lysozyme. Biochemistry 1994;33:5867-5876.
45. Morgan CJ, Miranker A, Dobson CM. Characterization of collapsed states in the early stages of the refolding of hen lysozyme. Biochemistry 1998;37:8473-8480.
46. Kuwajima K. The molten globule state ofa-lactalbumin. FASEB J 1996;10:102-109.
47. Pfeil W. Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin. Proteins 1998;30:43-48.
48. Sosnick TR, Shtilerman MD, Mayne L, Englander SW. Ultrafast signals in protein folding and the polypeptide contracted state. Proc Natl Acad Sci USA 1997;94:8545-8550.
49. Silow M, Oliveberg M. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc Natl Acad Sci USA 1997;94:6084-6086.
50. Ikeguchi M, Fujino M, Kato M, Kuwajima K, Sugai S. Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond. Protein Sci 1998;7:1564-1574.
51. Griko YV, Freire E, Privalov G, Van Dael H, Privalov PL. The unfolding thermodynamics of c-type lysozyme: A calorimetric study of the heat denaturation of equine lysozyme. J Mol Biol 1995;252:447-459.
52. Mizuguchi M, Masaki K, Demura M, Nitta K. Local and longrange interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin. J Mol Biol 2000;298:985-995.
53. Griko YV. Energetic basis of structural stability in the molten globule state: α-lactalbumin. J Mol Biol 2000;297:1259-1268.
54. Wu LC, Kim PS. A specific hydrophobic core in the α-lactalbumin molten globule. J Mol Biol 1998;280:175-182.
55. Song J, Bai P, Luo L, Peng Z-Y. Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule. J Mol Biol 1998;280:167-174.