Influence of Trp mutation on native, intermediate, and transition states of goat α-lactalbumin: An equilibrium and kinetic study

Biochemistry

Volumn 44, Issue 46, 2005, Pages 15129-15138

  Chedad, A ^a   Van Dael, H ^a   Vanhooren, A ^a   Hanssens, I ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; MUTAGENESIS; REACTION KINETICS;

MUTATION; TRANSITION STATES; TRYPTOPHAN;

PROTEINS;

ALPHA LACTALBUMIN; PHENYLALANINE; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; FLUORESCENCE; GENE MUTATION; GOAT; HYDROPHOBICITY; KINETICS; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ANIMALS; CIRCULAR DICHROISM; GOATS; GUANIDINE; HYDROPHOBICITY; KINETICS; LACTALBUMIN; MATHEMATICS; POINT MUTATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

CAPRA HIRCUS;

EID: 28044462676     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0512400     Document Type: Article

References (49)

1. Ptitsyn, O. B., Pain, R. H., Semitsonov, O. V., Zerovnik, E., and Razgulyaev, O. I. (1990) Evidence for a molten globule state as a general intermediate in protein folding, FEBS Lett. 262, 20-24.
2. Sanchez, I. E., and Kiefhaber, T. (2003) Evidence for sequential barriers and obligatory intermediates in apparent two-state folding, J. Mol. Biol. 325, 367-376.
3. Radford, S., Dobson, C., and Evans, P. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways, Nature 358, 302-307.
4. Van Dael, H. (1998) Chimeras of human lysozyme and α-lactalbumin: An interesting tool for studying partially folded states during protein folding, Cell. Mol. Life Sci. 54, 1217-1230.
5. Gunasekaran, K., Eyles, S. J., Hagler, A. T., and Gierasch, L. M. (2001) Keeping it in the family: Folding studies of related proteins, Curr. Opin. Struct. Biol. 11, 83-93.
6. Acharya, K. R., Stuart, D. I., Walker, N. P., Lewis, M., and Phillips, D. C. (1989) Refined structure of baboon α-lactalbumin at 1.7 Å resolution. Comparison with C-type lysozyme, J. Mol. Biol. 208, 99-127.
7. Pike, A. C. W., Brew, K., and Acharya, K. R. (1996) Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase, Structure 4, 691-703.
8. Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure, Proteins 6, 87-103.
9. Chyan, C. L., Wormald, C., Dobson, C. M., Evans, P. A., and Baum, J. (1993) Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study, Biochemistry 32, 5681-5691.
10. Arai, M., and Kuwajima, K. (1996) Rapid formation of a molten globule intermediate in refolding of α-lactalbumin, Folding Des. 1, 275-287.
11. Yoda, T., Saito, M., Arai, M., Horii, K., Tsumoto, K., Matsushima, M., Kumagai, I., and Kuwajima, K. (2001) Folding-unfolding of goat α-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations, Proteins 42, 49-65.
12. Ikeguchi, M., Kuwajima, K., Mitani, M., and Sugai, S. (1986) Evidence for the identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme, Biochemistry 25, 6965-6972.
13. Redfield, C. (2004) Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins, Methods 34, 121-132.
14. Matouschek, A., Kellis, J. T., Jr., Serrano, L., Bycroft, M., and Fersht, A. R. (1990) Transient folding intermediates characterized by protein engineering, Nature 346, 440-445.
15. Khorasanizadeh, S., Peters, I. D., and Roder, H. (1996) Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues, Nat. Struct. Biol. 3, 193-205.
16. Spudich, G. M., Miller, E. J., and Marqusee, S. (2004) Destabilization of the Escherichia coli RNase H kinetic intermediate: Switching between a two-state and three-state folding mechanism, J. Mol. Biol. 335, 609-618.
17. Friel, C. T., Beddard, G. S., and Radford, S. E. (2004) Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design, J. Mol. Biol. 342, 261-273.
18. Chedad, A., and Van Dael, H. (2004) Kinetics of folding and unfolding of goat α-lactalbumin, Proteins 57, 345-356.
19. Ishikawa, N., Chiba, T., Chen, L. T., Shimizu, A., Ikeguchi, M., and Sugai, S. (1998) Remarkable destabilization of recombinant α-lactalbumin by an extraneous N-terminal methionyl residue, Protein Eng. 11, 333-335.
20. Chaudhuri, T. K., Horii, K., Yoda, T., Arai, M., Nagata, S., Terada, T. P., Uchiyama, H., Ikura, T., Tsumoto, K., Kataoka, H., Matsushima, M., Kuwajima, K., and Kumagai, I. (1999) Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli, J. Mol. Biol. 285, 1179-1194.
21. Vanhooren, A., Chedad, A., Farkas, V., Majer, Z., Joniau, M., Van Dael, H., and Hanssens, I. (2005) Tryptophan to phenylalanine substitutions allow differentiation of short and long range conformational changes during denaturation of goat α-lactalbumin, Proteins 60, 118-130.
22. Loewenthal, R., Sancho, J., and Fersht, A. R. (1991) Fluorescence spectrum of barnase-contributions of three tryptophan residues and a histidine related pH dependence, Biochemistry 30, 6775-6779.
23. Locke, B. C., MacInnis, J. M., Qian, S. J., Gordon, J. I., Li, E., Fleming, G. R., and Yang, N. C. (1992) Fluorescence studies of rat cellular retinol binding protein-II produced in E. coli: An analysis of four tryptophan substitution mutants, Biochemistry 31, 2376-2383.
24. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturaion curves, Methods Enzymol. 131, 266-280.
25. Mizuguchi, M., Arai, M., Ke, Y., Nitta, K., and Kuwajima, K. (1998) Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy, J. Mol. Biol. 283, 265-277.
26. Saeki, K., Arai, M., Yoda, T., Nakao, M., and Kuwajima, K. (2004) Localized nature of the transition-state structure in goat α-lactalbumin folding, J. Mol. Biol. 341, 589-604.
27. Woody, R. W. (1994) Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins, Eur. Biophys. J. 23, 253-262.
28. Van Dael, H., Chedad, A., Vanhooren, A., and Hanssens, I. (2005) Influence of experimental conditions and Trp mutations on the stability and the folding characteristics of goat α-lactalbumin, J. Mol. Struct. 744-747, 155-160.
29. Eftink, M. R. (2000) Use of fluorescence spectroscopy as thermodynamics tool, Methods Enzymol. 323, 459-473.
30. Karplus, M., and Weaver, D. L. (1976) Protein-folding dynamics, Nature 260, 404-406.
31. Jacob, M., Schindler, T., Balbach, J., and Schmid, F. X. (1997) Diffusion control in an elementary protein folding reaction, Proc. Natl. Acad. Sci. U.S.A. 94, 5622-5627.
32. Kawahara, K., and Tanford, C. (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride, J. Biol. Chem. 241, 3228-3232.
33. Jacob, M., and Schmid, F. X. (1999) Protein folding as a diffusional process, Biochemistry 38, 13773-13779.
34. Silow, M., and Oliveberg, M. (1997) High energy channelling in protein folding, Biochemistry 36, 7633-7637.
35. Clarke, J., Hamill, S. J., and Johnson, C. M. (1997) Folding and stability of a fibronectin type III domain of human tenascin, J. Mol. Biol. 270, 771-778.
36. Dalby, P. A., Oliveberg, M., and Fersht, A. R. (1998) Movement of the intermediate and rate determining transition state of barnase on the energy landscape with changing temperature, Biochemistry 37, 4674-4679.
37. Otzen, D. E., Kristensen, O., Proctor, M., and Oliveberg M. (1999) Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots, Biochemistry 38, 6499-6511.
38. Fersht, A. R. (2000) A kinetically significant intermediate in the folding of barnase, Proc. Natl. Acad. Sci. U.S.A. 97, 14121-14126.
39. Bachmann, A., and Kiefhaber, T. (2001) Apparent two-state Tendamistat folding is a sequential process along a defined route, J. Mol. Biol. 306, 375-386.
40. Engman, K. C., Sandberg, A., Leckner, J., and Karlsson, B. G. (2004) Probing the influence on folding behaviour of structurally conserved core residues in P. aeruginosa apo-azurin, Protein Sci. 13, 2706-2715.
41. Sandberg, A., Leckner, J., and Karlsson, B. G. (2004) Apo-azurin folds via an intermediate that resembles the molten globule, Protein Sci. 13, 2628-2638.
42. Sanchez, I. E., and Kiefhaber, T. (2003) Hammond behaviour versus ground-state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states, J. Mol. Biol. 327, 867-884.
43. Bollen, Y. J. M., Sanchez, I. E., and van Mierlo, C. P. M. (2004) Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin, Biochemistry 43, 10475-10489.
44. Fersht, A. R. (1999) Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding, p 631, W. H. Freeman and Co., New York.
45. 2+-induced alteration in the unfolding behaviour of α-lactalbumin, J. Biochem. 99, 1191-1201.
46. Haezebrouck, P., Noyelle, K., Joniau, M., and Van Dael, H. (1999) Kinetic and equilibrium intermediate states are different in LYLA1, a chimera of lysozyme and α-lactalbumin, J. Mol. Biol. 295, 703-718.
47. Mogensen, J. E., Ipsen, H., Holm, J., and Otzen, D. (2004) Elimination of a misfolded folding intermediate by a single point mutation, Biochemistry 43, 3357-3367.
48. Ikeguchi, M., Fujino, M., Kato, M., Kuwajima, K., and Sugai, S. (1998) Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond, Protein Sci. 7, 1564-1574.
49. Guex, N., and Peitsch, M. C. (1997) Swiss-model and the Swiss-PDB viewer: An environment for comparative protein modelling, Electrophoresis 18, 2714-2723.