Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering

Protein Science

Volumn 6, Issue 2, 1997, Pages 422-430

  Kataoka, Mikio ^a   Kuwajima, Kunihiro ^b   Tokunaga, Fumio ^a   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

compact denatured state; molecular compactness; molten globule; protein folding; solution X ray scattering; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; APOPROTEIN;

ARTICLE; DISULFIDE BOND; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; RADIATION SCATTERING;

EID: 0031050429     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060219     Document Type: Article

References (71)

1. Acharya KR, Stuart DI, Walker NPC, Lewis M, Phillips DC. 1989. Refined structure of baboon α-lactalbumin at 1.7Å resolution. Comparison with c-type lysozyme. J Mol Biol 208:99-127.
2. Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. 1993. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study. Biochemistry 32:1707-1718.
3. Baum J, Dobson CM, Evans PA, Hanley C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry 28:7-13.
4. Carra JH, Anderson EA, Privalov PL. 1994. Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry 33:10842-10850.
5. Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J. 1993. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study. Biochemistry 32:5681-5691.
6. Creighton TE, Darby N, Kemmink J. 1996. The roles of partly folded intermediates in protein folding. FASEB J 10:110-118.
7. Damaschun G, Damaschun H, Gast K, Gernat C, Zirwer D. 1991. Acid denatured apo-cytochrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering. Biochim Biophys Acta 1078:289-295.
8. Damaschun G, Damaschun H, Gast K, Misselwitz R, Müller JJ, Pfeil W, Zirwer D. 1993. Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast. Biochemistry 32:7739-7746.
9. Dill KA, Shortle D. 1991. Denatured states of proteins. Annu Rev Biochem 60:795-825.
10. Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bychkova VE, Gilmanshin RI, Lebedev YO, Semisotnov GV, Tiktopulo EI, Ptitsyn OB. 1985. Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin. Eur Biophys J 13:109-121.
11. Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotnov GV, Venyaminov SY, Ptitsyn OB. 1981. α-Lactalbumin: Compact state with fluctuating tertiary structure? FEBS Letters 136:311-315.
12. Doniach S, Bascle J, Garel T, Orland H. 1995. Partially folded states of proteins: Characterization by X-ray scattering. J Mol Biol 254:960-967.
13. Ermácora MR, Ledman DW, Fox RO. 1996. Mapping the structure of a non-native state of staphylococcal nuclease. Nature Struct Biol 3:59-65.
14. Ewbank JJ, Creighton TE. 1991. The molten globule protein conformation probed by disulphide bonds. Nature 350:518-520.
15. Fersht AR. 1995. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873.
16. Fink AL. 1995. Compact intermediate states in protein folding. Annu Rev Biophys Biomol Struct 24:495-522.
17. Flanagan JM, Kataoka M, Fujisawa T, Engelman DM. 1993. Mutation can cause large changes in the conformation of a denatured protein. Biochemistry 32:10359-10370.
18. Flanagan JM, Kataoka M, Shortle D, Engelman DM. 1992. Truncated staphylococcal nuclease is compact but disordered. Proc Natl Acad Sci USA 89:748-752.
19. Gast K, Damaschun H, Misselwitz R, Müller-Frohne M, Zirwer D, Damaschun G. 1994. Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate. Eur Biophys J 23:297-305.
20. Gast K, Zirwer D, Welfle H, Bychkova VE, Ptitsyn OB. 1986. Quasielastic light scattering from human alpha-lactalbumin: Comparison of molecular dimensions in native and "molten globule" states. Int J Biol Macromol 8:231-236.
21. Gittis AG, Stites WE, Lattman EE. 1993. The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. J Mol Biol 232:718-724.
22. Glatter O, Kratky O. 1982. Small angle X-ray scattering. New York: Academic Press.
23. Griko Y, Freire E, Privalov PL. 1994b, Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
24. Griko Y, Gittis A, Lattman EE, Privalov PL. 1994a. Residual structure in a staphylococcal nuclease fragment: Is it a molten globule and is its unfolding a first-order phase transition? J Mol Biol 243:93-99.
25. Guinier A, Fournet B. 1955. Small-angle scattering of X-rays. New York: John Wiley.
26. Hagihara Y, Tan Y, Goto Y. 1994. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c: Effects of acetylation, heat, urea, and guanidine-hydrochloride. J Mol Biol 237:336-348.
27. Hamada D, Hoshino M, Kataoka M, Fink AL, Goto Y. 1993. Intermediate conformational states of apocytochrome c. Biochemistry 32:10351-10358.
28. Hamada D, Kidokoro S, Fukada H, Takahashi K, Goto Y. 1994. Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc Natl Acad Sci USA 91:10325-10329.
29. Hamada D, Kuroda Y, Kataoka M, Aimoto S, Yoshimura T, Goto Y. 1996. Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J Mol Biol 256:172-186.
30. Hughson FM, Wright PE, Baldwin RL. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
31. Izumi Y, Miyake Y, Kuwajima K, Sugai S, Inoue K, Iizumi M, Katano S. 1983. Folding-unfolding of α-lactalbumin. Physica 120B:444-448.
32. Kataoka M, Flanagan JM, Tokunaga F, Engelman DM. 1994. Use of X-ray solution scattering for protein folding study. In: Chance B, Deisenhofer J, Ebashi S, Goodhead DT, Helliwell JR, Huxley HE, Iizuka T, Kirz J, Mitsui T, Rubenstein E, Sakabe N, Sasaki T, Schmahl G, Stuhrmann HB, Wüthrich K, Zaccai G, eds. Synchrotron radiation in the biosciences. Oxford: Clarendon Press. pp. 187-194.
33. Kataoka M, Hagihara Y, Mihara K, Goto Y. 1993. Molten globule of cytochrome c studied by the small angle X-ray scattering. J Mol Biol 229:591-596.
34. Kataoka M, Head JF, Persechini A, Kretsinger RH, Engelman DM. 1991. Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker has a predominantly α-helical conformation. Biochemistry 30:1188-1192.
35. Kataoka M, Goto Y. 1996. X-ray solution scattering studies of protein folding. Folding & Design 1:R107-R114.
36. Kataoka M, Nishii I, Fujisawa T, Ueki T, Tokunaga F, Goto Y. 1995. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J Mol Biol 249:215-228.
37. Kendrew JC, Dickerson RE, Strandberg BE, Hart RG, Davies DR, Phillips DC, Shore VC. 1960. Structure of myoglobin - Three-dimensional Fourier synthesis at 2Å resolution. Nature 185:422-427.
38. Konno T, Kataoka M, Kamatari Y, Kanaori K, Nosaka A, Akasaka K. 1995. Solution X-ray scattering analysis of cold-heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor. J Mol Biol 257:95-103.
39. Kratky O. 1982. Natural high polymers in the dissolved and solid state. In: Glatter O, Kratky O. eds. Small angle X-ray scattering. New York: Academic Press. pp. 361-386.
40. Kuroda Y, Kidokoro S, Wada A. 1992. Thermodynamic characterization of cytochrome c at low pH. J Mol Biol 223:1139-1153.
41. Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct Funct Genet 6:87-103.
42. Kuwajima K. 1996. The molten globule state of α-lactalbumin. FASEB J 10:102-109
43. Kuwajima K, Hiraoka Y, Ikeguchi M, Sugai S. 1985. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24:874-881.
44. Kuwajima K, Nitta K, Yoneyama M, Sugai S. 1976. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J Mol Biol 106:359-373.
45. Lattman EE. 1994. Small angle scattering studies of protein folding. Curr Opin Struct Biol 4:87-92.
46. Lattman EE, Fiebig KM, Dill KA. 1994. Modeling compact denatured states of proteins. Biochemistry 33:6158-6166.
47. Loh SN, Kay MS, Baldwin RL. 1995. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc Natl Acad Sci USA 92:5446-5450.
48. Moore PB. 1980. Small-angle scattering: Information content and error analysis. J Appl Crystallog 13:168-175.
49. Nishii I, Kataoka M, Goto Y. 1995. Thermodynamic stability of the molten globule states of apomyoglobin. J Mol Biol 250:223-238.
50. Nishii I, Kataoka M, Tokunaga F, Goto Y. 1994. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 53:4903-4909.
51. Ohgushi M, Wada A 1983. "Molten-globule state": A compact form of globular proteins with mobile side chains. FEBS Letters 164:21-24.
52. Okazaki A, Ikura T, Nikaido K, Kuwajima K. 1994. The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nature Struct Biol 1:439-445.
53. Olah GA, Trakhanov S, Trewhella J, Quiocho FA. 1993. Leucine/isoleucine/valine binding protein contracts upon binding of ligand. J Biol Chem 268: 16241-16247.
54. Peng Z-Y, Kim PS. 1994. A protein dissection study of a molten globule. Biochemistry 33:2136-2141.
55. Potekhin S, Pfeil W. 1989. Microcalorimetric studies of conformational transitions of ferricytochrome c in acidic solution. Biophys Chem 34:55-62.
56. Privalov PL. 1996. Intermediate states in protein folding. J Mol Biol 258:707-725.
57. Ptitsyn OB. 1987. Protein folding: Hypotheses and experiments. J Prot Chem 6:273-293.
58. Ptitsyn OB. 1992. The molten globule state. In: Creighton EE., ed. Protein folding. New York: W. H. Freeman and Company. pp. 243-400.
59. Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47: 83-229.
60. Roder H, Elöve GA, Englander SW. 1988. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335:700-704.
61. Schulman BA, Redfield C, Peng Z-Y, Dobson CM, Kim PS. 1995. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J Mol Biol 253:651-657.
62. Shortle D. 1996. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J 10:27-34.
63. Shortle D, Abeygunawardana C. 1993. NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure 1:121-134.
64. Sosnick TR, Mayne L, Hiller R, Englander SW. 1994. The barriers in protein folding. Nature Struct Biol 1:149-156.
65. Sosnick TR, Trewhella J. 1992. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry 31:8329-8335.
66. Svergun DI, Semenyuk AV, Feigin LA. 1988. Small-angle-scattering data treatment by the regularization method. Acta Crystallog sect A 44:244-250.
67. Ueki T. 1991. Biopolymers and solution X-ray scattering. Is it useful in structural research in biology? Nucl Instrum Meth Phys Res A303:464-475.
68. Xie D, Bhakuni V, Freire E. 1991. Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-α-lactalbumin. Biochemistry 30:10673-10678.
69. Xie D, Bhakuni V, Freire E. 1993. Are the molten globule and the unfolded states of apo-α-lactalbumin enthalpically equivalent? J Mol Biol 232:5-8.
70. Yutani K, Ogasahara K, Kuwajima K. 1992. The absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study by differential scanning microcalorimetry. J Mol Biol 228:347-350.
71. Zimm B. 1948. The scattering of light and the radial distribution function of high polymer solutions. J Chem Phys 16:1093-1099.