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Small Angle X-Ray Scattering from Lipid-Bound Myelin Basic Protein in Solution

H. Haas^*, C. L. P. Oliveira, I. L. Torriani, E. Polverini, A. Fasano^¶, G. Carlone^¶, P. Cavatorta and P. Riccio^||

^* Universidade de São Paulo-Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Ribeirão Preto, Brazil; Instituto de Fisica, Laboratório de Cristalografia Aplicada e Raios X, Universidade Estadual de Campinas, Brazil; Laboratório Nacional de Luz Síncrotron, Campinas, Brazil; Dipartimento di Fisica and Istituto Nazionale per la Fisica della Materia, University of Parma, Parma, Italy; ^¶ Dipartimento di Biochimica e Biologia Molecolare, University of Bari, Bari, Italy; and ^|| Dipartimento di Biologia, Difesa e Biotecnologie Agro-forestali, University of Basilicata, Potenza, Italy

Correspondence: Address reprint requests to P. Riccio, E-mail: riccio{at}unibas.it.

The structure of myelin basic protein (MBP), purified from the myelin sheath in both lipid-free (LF-MBP) and lipid-bound (LB-MBP) forms, was investigated in solution by small angle x-ray scattering. The water-soluble LF-MBP, extracted at pH < 3.0 from defatted brain, is the classical preparation of MBP, commonly regarded as an intrinsically unfolded protein. LB-MBP is a lipoprotein-detergent complex extracted from myelin with its native lipidic environment at pH > 7.0. Under all conditions, the scattering from the two protein forms was different, indicating different molecular shapes. For the LB-MBP, well-defined scattering curves were obtained, suggesting that the protein had a unique, compact (but not globular) structure. Furthermore, these data were compatible with earlier results from molecular modeling calculations on the MBP structure which have been refined by us. In contrast, the LF-MBP data were in accordance with the expected open-coil conformation. The results represent the first direct structural information from x-ray scattering measurements on MBP in its native lipidic environment in solution.

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