Conformation of bovine myelin basic protein purified with bound lipids

European Biophysics Journal

Volumn 28, Issue 4, 1999, Pages 351-355

  Polverini, Eugenia ^a   Fasano, Anna ^b   Zito, Francesco ^b   Riccio, Paolo ^c   Cavatorta, Paolo ^a  

^a UNIVERSITY OF PARMA   (Italy)

^b UNIVERSITY OF BARI   (Italy)

^c UNIVERSITY OF BASILICATA   (Italy)

Author keywords

Circular dichroism; Computational predictive methods; Lipid protein interaction; Myelin basic protein; Protein structure

Indexed keywords

DETERGENT; LIPID; MYELIN BASIC PROTEIN;

ANIMAL TISSUE; ARTICLE; CATTLE; CIRCULAR DICHROISM; MYELIN SHEATH; NONHUMAN; PREDICTION; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; BIOPHYSICS; CATTLE; CIRCULAR DICHROISM; LIPIDS; MOLECULAR SEQUENCE DATA; MYELIN BASIC PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0032974494     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050218     Document Type: Article

References (47)

1. Bhaskaran R, Ponnuswamy PK (1984) Dynamics of amino acid residues in globular proteins. Int J Pept Protein Res 24:180-191
2. Bobba A, Munno I, Greco B, Pellegrino NM, Riccio P, Jirillo E, Quagliariello E (1991) On the spontaneous adherence of myelin basic protein to T lymphocytes. Biochem Biophys Res Commun 180:1125-1129
3. Burns PF, Campagnoni CW (1983) Interaction of the mouse and bovine myelin basic protein and two cleavage fragments with anionic detergents. Biochim Biophys Acta 743:379-388
4. Burns PF, Campagnoni CW, Chaiken IM, Campagnoni AT (1981) Interaction of free and immobilized myelin basic protein with anionic detergents. Biochemistry 20:2463-2469
5. Cavatorta P, Casali E, Sartor G (1986) The problem of light scattering in the absorbance and fluorescence studies of proteins in membranes. In: Azzi A (ed) Membrane proteins. Springer, Berlin Heidelberg New York, pp 24-31
6. Cavatorta P, Masotti L, Szabo AG, Juretic D, Riccio P, Quagliariello E (1988) Fluorescence spectral resolution of myelin basic protein conformers in complexes with lysophosphatidylcholine. Cell Biophys 13:201-215
7. Chou PY, Fasman GD (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 47:145-148
8. Deibler GE, Martenson RE, Kies MW (1972) Large-scale preparation of myelin basic protein from central nervous tissue of several mammalian species. Prep Biochem 2:139-165
9. Deibler GE, Boyd LF, Kies MW (1984) Proteolitic activity associated with purified myelin basic protein. In: Alvord EC Jr, Kies MW, Suckling AJ (eds) Experimental allergic encephalomyelitis: a useful model for multiple sclerosis. Liss, New York, pp 249-256
10. Deleage G, Roux B (1987) An algorithm for protein secondary structure prediction based on class prediction. Protein Eng 1:289-294
11. DiFrancesco V, Munson PJ, Garnier J (1995) Use of multiple alignments in protein secondary structure prediction. 28th Hawaii International Conference on System Sciences, vol 5. IEEE, Los Alamitos, Calif., pp 285-291
12. Eisenberg D, Schwarz E, Komarony M, Wall R (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179:125-142
13. Folch J, Lees M, Sloane-Stanley GH (1957) A simple method for the isolation and purification of total lipids from animal tissue. J Biol Chem 226:497-509
14. Frishman D, Argos P (1995) Knowledge-based secondary structure assignment. Proteins Struct Funct Genet 23:566-579
15. Garnier J, Gibrat JF, Robson B (1996) GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol 266:540-553
16. Geourjon C, Deleage G (1995) SOPMA: significant improvements in protein secondary structure prediction by prediction from multiple alignments. Comput Appl Biosci 11:681-684
17. Gibrat JF, Gamier J, Robson B (1987) Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs. J Mol Biol 198:425-443
18. Janin J (1979) Surface and inside volumes in globular proteins. Nature 277:491-492
19. Kawabata T, Doi J (1997) Improvement of protein secondary structure prediction using binary word encoding. Proteins 27:36-46
20. Kneller DG, Cohen FE, Langridge R (1990) Improvements in protein secondary structure prediction by an enhanced neural network. J Mol Biol 214:171-182
21. Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
22. Levin JM, Robson B, Garnier J (1986) An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Lett 205:303-308
23. Levitt M (1978) Conformational preferences of amino acids in globular proteins. Biochemistry 17:4277-4285
24. Liebes LR, Phillips WD (1975) Solution behaviour, circular dichroism and 220 MHz PMR studies of the bovine myelin basic protein. Biochim Biophys Acta 405:27-39
25. Liuzzi GM, Tamborra R, Ventola A, Bisaccia F, Quagliarello E, Riccio P (1996) Different recognition by clostripain of myelin basic protein in the lipid-free and lipid-bound forms. Biochem Biophys Res Commun 226:566-571
26. Lolli F, Liuzzi GM, Vergelli M, Massacesi L, Ballerini C, Amaducci L, Riccio P (1993) Antibodies specific forthe lipid-bound form of myelin basic protein during experimental autoimmune encephalomyelitis. J Neuroimmunol 44:69-76
27. Martenson RE (1986) Possible hydrophobic region in myelin basic protein consisting of an orthogonally packed β-sheet. J Neurochem 46:1612-1622
28. Martenson RE (1992) Myelin: biology and chemistry. CRC Press, Boca Raton, Fla
29. Massacesi L, Vergelli M, Zehetbauer B, Liuzzi GM, Olivotto J, Ballerini C, Uccelli A, Mancardi L, Riccio P, Amaducci L (1993) Induction of experimental autoimmune encephalomyelitis in rats and immune response to myelin basic protein in lipid-bound form. J Neurol Sci 119:91-98
30. Mazzanti B, Vergelli M, Riccio P, Martin R, McFarland HF, Liuzzi MG, Amaducci L, Massacesi L (1998) T cell response to myelin basic protein and lipid-bound myelin basic protein in patients with multiple sclerosis and healthy donors. J Neuroimmunol 82:96-100
31. Mendz GL, Moore WJ, Brown LR, Martenson RE (1984) Interaction of myelin basic protein with micelles of dodecylphosphocholine. Biochemistry 23:6041-6046
32. Mendz GL, Brown LR, Martenson RE (1990) Interactions of myelin basic protein with mixed dodecylphosphocholine/palmitoyllysophosphatidic acid micelles. Biochemistry 29:2304-2311
33. Perczel A, Hollosi M, Tusnady G, Fasman GD (1991) Convex constraint analysis: a natural deconvolution of circular dichroism curves of proteins. Protein Eng 4:669-679
34. Perczel A, Park K, Fasman GD (1992) Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide. Anal Biochem 203:83-93
35. Readhead C, Popko B, Takahashi N, Shine HD, Saavedra RA, Sidman RL, Hood L (1987) Expression of a myelin basic protein gene in transgenic mice: correction of the dysmyelinating phenotype. Cell 48:703-712
36. Riccio P, Rosenbusch JP, Quagliariello E (1984) A new procedure to isolate brain myelin basic protein in a lipd-bound form. FEBS Lett 177:236-240
37. Riccio P, Masotti L, Cavatorta P, Santis AD, Juretic D, Bobba A, Pasquali-Ronchetti I, Quagliariello E (1986) Myelin basic protein ability to organize lipid bilayers: structural transition in bilayers of lysophosphatidylcholine micelles. Biochem Biophys Res Commun 134:313-319
38. Riccio P, Liuzzi GM, Quagliariello E (1990) Lipid-bound native-like myelin basic protein: batch-wise preparation and perspectives for use in demyelinating disease. Mol Chem Neuropathol 13:185-194
39. Riccio P, Bobba A, Romito E, Minetola M, Quagliariello E (1994) A new detergent to purify CNS myelin basic protein isoforms in lipid-bound form. NeuroReport 5:689-692
40. Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G (1997) Three-dimensional structure of myelin basic protein. II. Molecular modeling and consideration of predicted structures in multiple sclerosis. J Biol Chem 272:4269-4275
41. Rost B, Sander C (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72
42. Smith R (1992) The basic protein of CNS myelin: its structure and ligand binding. J Neurochem 59:1589-1608
43. Smith R, McDonald BJ (1979) Association of myelin basic protein with detergent micelles. Biochim Biophys Acta 554:133-147
44. Stoner GL (1984) Predicted folding of β-structure in myelin basic protein. J Neurochem 43:433-447
45. Stoner GL (1990) Conservation throughout vertebrate evolution of the predicted β-strands in myelin basic protein. J Neurochem 55:1404-1411
46. Stuart BH (1996) A Fourier transform infrared spectroscopy study of the secondary structure of myelin basic protein in reconstituted myelin. Biochem Mol Biol Int 38:839-845
47. Vergelli M, Pinet V, Vogt AB, Kalbus M, Malnati M, Riccio P, Long EO, Martin R (1997) HLA-DR-restricted presentation of purified myelin basic protein is independent of intracellular processing. Eur J Immunol 27:941-951