Organization and dynamics of tryptophans in the molten globule state of bovine α-lactalbumin utilizing wavelength-selective fluorescence approach: Comparisons with native and denatured states

Biochemical and Biophysical Research Communications

Volumn 394, Issue 4, 2010, Pages 1082-1086

  Chaudhuri, Arunima ^a   Haldar, Sourav ^a   Chattopadhyay, Amitabha ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

Lactalbumin; Fluorescence anisotropy; Fluorescence lifetime; Molten globule; Protein conformation; Red edge excitation shift

Indexed keywords

ALPHA LACTALBUMIN; SOLVENT; TRYPTOPHAN;

AMINO ACID ANALYSIS; ANISOTROPY; ARTICLE; CHEMICAL PHENOMENA; DENATURATION; ENVIRONMENT; FLUORESCENCE; MOTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RED EDGE EXCITATION SHIFT; SPECTRAL SENSITIVITY; STRUCTURE ANALYSIS;

ANIMALS; CATTLE; CIRCULAR DICHROISM; FLUORESCENCE; LACTALBUMIN; LUMINESCENT MEASUREMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; TRYPTOPHAN;

BOVINAE;

EID: 77950862614     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.03.130     Document Type: Article

References (36)

1. Xie H., Vucetic S., Iakoucheva L.M., et al. Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. J. Proteome Res. 6 (2007) 1882-1898
2. Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
3. Dunker A.K., Silman I., Uversky V.N., et al. Function and structure of inherently disordered proteins. Curr. Opin. Struct. Biol. 18 (2008) 756-764
4. Dolgikh D.A., Gilmanshin R.I., Brazhnikov E.V., et al. α-Lactalbumin: compact state with fluctuating tertiary structure?. FEBS Lett. 136 (1981) 311-315
5. Ohgushi M., and Wada A. 'Molten-globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett. 164 (1983) 21-24
6. Kuwajima K. The molten globule state of α-lactalbumin. FASEB J. 10 (1996) 102-109
7. Permyakov E.A., and Berliner L.J. α-Lactalbumin: structure and function. FEBS Lett. 473 (2000) 269-274
8. Chrysina E.D., Brew K., and Acharya K.R. Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions. J. Biol. Chem. 275 (2000) 37021-37029
9. Vanhooren A., Illyes E., Majer Z., et al. Fluorescence contributions of the individual Trp residues in goat α-lactalbumin. Biochim. Biophys. Acta 1764 (2006) 1586-1591
10. Grobler J.A., Wang M., Pike A.C., et al. Study by mutagenesis of the roles of two aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system. J. Biol. Chem. 269 (1994) 5106-5114
11. Vanhooren A., Chedad A., Farkas V., et al. Tryptophan to phenylalanine substitutions allow differentiation of short- and long-range conformational changes during denaturation of goat α-lactalbumin. Proteins 60 (2005) 118-130
12. Mukherjee S., and Chattopadhyay A. Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems. J. Fluoresc. 5 (1995) 237-246
13. Chattopadhyay A. Exploring membrane organization and dynamics by the wavelength-selective fluorescence approach. Chem. Phys. Lipids 122 (2003) 3-17
14. Raghuraman H., Kelkar D.A., and Chattopadhyay A. Novel insights into protein structure and dynamics utilizing the red edge excitation shift. In: Geddes C.D., and Lakowicz J.R. (Eds). Reviews in Fluorescence vol. 2 (2005), Springer, New York 199-222
15. Demchenko A.P. Site-selective red-edge effects. Methods Enzymol. 450 (2008) 59-78
16. Haldar S., and Chattopadhyay A. Dipolar relaxation within the protein matrix of the green fluorescent protein: a red edge excitation shift study. J. Phys. Chem. B 111 (2007) 14436-14439
17. Guha S., Rawat S.S., Chattopadhyay A., et al. Tubulin conformation and dynamics: a red edge excitation shift study. Biochemistry 35 (1996) 13426-13433
18. Chattopadhyay A., Rawat S.S., Kelkar D.A., et al. Organization and dynamics of tryptophan residues in erythroid spectrin: novel structural features of denatured spectrin revealed by the wavelength-selective fluorescence approach. Protein Sci. 12 (2003) 2389-2403
19. Raghuraman H., and Chattopadhyay A. Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution. Biopolymers 83 (2006) 111-121
20. Rawat S.S., Kelkar D.A., and Chattopadhyay A. Monitoring gramicidin conformations in membranes: a fluorescence approach. Biophys. J. 87 (2004) 831-843
21. Raghuraman H., and Chattopadhyay A. Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach. Langmuir 19 (2003) 10332-10341
22. Kelkar D.A., and Chattopadhyay A. Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach. Biophys. J. 88 (2005) 1070-1080
23. Wyttenbach T., and Bowers M.T. Hydration of biomolecules. Chem. Phys. Lett. 480 (2009) 1-16
24. Engel M.F., Van Mierlo C.P., and Visser A.J. Kinetic and structural characterization of adsorption-induced unfolding of bovine α-lactalbumin. J. Biol. Chem. 277 (2002) 10922-10930
25. Haldar S., Raghuraman H., and Chattopadhyay A. Monitoring orientation and dynamics of membrane-bound melittin utilizing dansyl fluorescence. J. Phys. Chem. B 112 (2008) 14075-14082
26. Lakowicz J.R. Principles of Fluorescence Spectroscopy. third ed. (2006), Springer, New York
27. 2+ and other divalent metal ions to bovine α-lactalbumin. J. Biol. Chem. 256 (1981) 8582-8587
28. Eftink M.R. Fluorescence techniques for studying protein structure. Methods Biochem. Anal. 35 (1991) 127-205
29. Nanda V., and Brand L. Aromatic interactions in homeodomains contribute to the low quantum yield of a conserved, buried tryptophan. Proteins 40 (2000) 112-125
30. Moens P.D., Helms M.K., and Jameson D.M. Detection of tryptophan to tryptophan energy transfer in proteins. Protein J. 23 (2004) 79-83
31. Mok K.H., Nagashima T., Day I.J., et al. Multiple subsets of side-chain packing in partially folded states of α-lactalbumins. Proc. Natl. Acad. Sci. USA 102 (2005) 8899-8904
32. Wijesinha-Bettoni R., Dobson C.M., and Redfield C. Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules. J. Mol. Biol. 312 (2001) 261-273
33. Weber G., and Shinitzky M. Failure of energy transfer between identical aromatic molecules on excitation at the long wave edge of the absorption spectrum. Proc. Natl. Acad. Sci. USA 65 (1970) 823-830
34. De Lauder W.B., and Wahl Ph. Effect of solvent upon the fluorescence decay of indole. Biochim. Biophys. Acta 243 (1971) 153-163
35. Krishna M.M.G., and Periasamy N. Fluorescence of organic dyes in lipid membranes: site of solubilization and effects of viscosity and refractive index on lifetimes. J. Fluoresc. 8 (1998) 81-91
36. Sen P., Mukherjee S., Dutta P., et al. Solvation dynamics in the molten globule state of a protein. J. Phys. Chem. B 107 (2003) 14563-14568