Is the molten globule a third thermodynamic state of protein? The example of α-lactalbumin

Proteins: Structure, Function and Genetics

Volumn 30, Issue 1, 1998, Pages 43-48

  Pfeil, Wolfgang ^a  

^a UNIVERSITY OF POTSDAM   (Germany)

Author keywords

lactalbumin; Calorimetry; Derivative spectroscopy; Molten globule; Viscosimetry

Indexed keywords

ALPHA LACTALBUMIN; PROTEIN;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; CALORIMETRY; CATTLE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN TERTIARY STRUCTURE; SPECTROSCOPY; THERMAL ANALYSIS; THERMODYNAMICS; VISCOMETRY;

ANIMALS; CATTLE; LACTALBUMIN; PROTEIN FOLDING; THERMODYNAMICS;

BOS TAURUS; BOVINAE;

EID: 0031963564     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<43::AID-PROT4>3.0.CO;2-L     Document Type: Article

References (39)

1. Kuwajima, K., Nitta, K., Yoneyama, M., Sugai, S. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106:359-373, 1974.
2. Kuwajima, K. A folding model of α-lactalbumin deduced from the three-state denaturation mechanism. J. Mol. Biol. 114:241-258, 1977.
3. Dolgikh, D.A., Gilmanshin, R.I., Brazhnikov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyaminov, S. Yu., Ptitsyn, O.B. α-Lactalbumin: Compact state with fluctuating tertiary structure? FEBS Lett. 136:311-315, 1981.
4. Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins 6:87-103, 1989.
5. Ptitsyn, O.B. The molten globule state. In: "Protein Folding." Creighton, T.R. (ed.). New York: W.H. Freeman, 1992:243-300.
6. Ptitsyn, O.B. Molten globule and protein folding. Adv. Protein Chem. 47:83-229, 1995.
7. Kuwajima, K. The molten globule state of α-lactalbumin. FASEB J. 10:102-109, 1996.
8. Pfeil, W. Thermodynamics of α-lactalbumin unfolding. Biophys. Chem. 13:181-186, 1981.
9. Pfeil, W., Sadowski, M.L. A scanning calorimetric study of bovine and human apo-α-lactalbumin. Studia Biophys. 109:163-170, 1985.
10. Pfeil, W., Bychkova, V.E., Ptitsyn, O.B. Physical nature of the phase transition in globular proteins: Calorimetric study of human α-lactalbumin. FEBS Lett. 198:287-291, 1986.
11. Xie, D., Bhakuni, V., Freire, E. Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-α-lactalbumin. Biochemistry 30:10673-10678, 1991.
12. Yutani, K., Ogasahara, K., Kuwajima, K. 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, 1992.
13. Griko, Yu. V., Freire, E., Privalov, P.L. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899, 1994.
14. Ptitsyn, O.B., Uversky, V.N. The molten globule is a third thermodynamical state of protein molecules. FEBS Lett. 341:15-18, 1994.
15. Uversky, V.N., Ptitsyn, O.B. All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Folding Design 1:117-122, 1996.
16. Sugai, S., Yashiro, H., Nitta, K. Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride. Biochim. Biophys. Acta 328:35-41, 1973.
17. Gekko, K., Hasegawa, Y. Compressibility-structure relationship of globular proteins. Biochemistry 25:6563-6571, 1986.
18. Sturtevant, J.M. Calorimetry. Methods Enzymol. 26:227-253, 1972.
19. Makhatadze, G.I., Privalov, P.L. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect. J. Mol. Biol. 213:375-384, 1990.
20. Makhatadze, G.I., Privalov, P.L. Energetics of protein structure. Adv. Protein Chem. 47:307-425, 1995.
21. Ragone, R., Colonna, G., Balestieri, C., Servillo, C., Irace, G. Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 23:1871-1875, 1984.
22. Mach, H., Middaugh, C.R. Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy. Anal. Biochem. 222:323-331, 1994.
23. Shakhnovich, E.I., Finkelstein, A.V. Theory of cooperative transitions in protein molecules. I. Why denaturation of globular proteins is a first-order phase transition. Biopolymers 28:1667-1680, 1989.
24. Finkelstein, A. V., Shakhnovich, E.I. Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers 28:1681-1694, 1989.
25. 1H NMR. Biochemistry 32:13198-13203, 1993.
26. Chyan, C.-L., Wormald, C., Dobson, C.M., Evans, P.A., Baum, J. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study. Biochemistry 32:5681-5691, 1993.
27. Schulman, B.A., Redfield, C., Peng, Z.-y., Dobson, C.M., Kim, P.S. 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, 1995.
28. Peng, Z.-y., Wu, L.C., Kim, P.S. Local structural preferences in the α-lactalbumin molten globule. Biochemistry 34:3248-3252, 1995.
29. Laureto, P.P. de, De Filippis, V., Di Bello, M., Zambonin, M., Fontana, A. Probing the molten globule state of α-lactalbumin by limited proteolysis. Biochemistry 34:12596-12604, 1995.
30. Schulman, B.A., Kim, P.S. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. Nature Struct. Biol. 3:682-687, 1996.
31. Wilson, G., Ford, S.J., Cooper, A., Hecht, L., Wen, Z.Q., Barron, L.D. Vibrational Raman optical activity of α-lactalbumin: Comparison with lysozyme, and evidence for native tertiary folds in molten globule states. J. Mol. Biol. 254:747-760, 1995.
32. Wilson, G., Hecht, L., Barron, L.D. The native-like tertiary fold in molten globule α-lactalbumin appears to be controlled by a continuous phase transition. J. Mol. Biol. 261:341-347, 1996.
33. Kharakoz, D.P., Bychkova, V.E. Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior. Biochemistry 36:1882-1890, 1997.
34. Uchiyama, H., Perez-Prat, E.M., Watanabe, K., Kumagai, I., Kuwajima, K. Effect of amino acid substitutions in the hydrophobic core of α-lactalbumin on the stability of the molten globule state. Protein Eng. 8:1153-1161, 1995.
35. Makhatadze, G.I., Privalov, P.L. Protein Interactions with urea and guanidinium chloride: A calorimetric study. J. Mol. Biol. 226:491-505, 1992.
36. Smith, J.S., Scholtz, J.M. Guanidine hydrochloride unfolding of peptide helices: Separation of denaturant and salt effects. Biochemistry 35:7292-7297, 1996.
37. Stigter, D., Alonso, D.O.V., Dill, K.A. Protein stability: Electrostatics and compact denatured states. Proc. Natl. Acad. Sci. U.S.A. 88:4176-4180, 1991.
38. Privalov, P.L. Intermediate states in protein folding. J. Mol. Biol. 258:707-725, 1996.
39. Ptitsyn, O. How molten is the molten globule? Nature Struct. Biol. 3:488-490, 1996.