Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/94225
Type: Artigo de periódico
Title: Small Angle X-ray Scattering From Lipid-bound Myelin Basic Protein In Solution
Author: Haas H.
Oliveira C.L.P.
Torriani I.L.
Polverini E.
Fasano A.
Carlone G.
Cavatorta P.
Riccio P.
Abstract: 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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Rights: aberto
Identifier DOI: 
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0347316424&partnerID=40&md5=d64ba9ae023bce090d9b8bf242b520cb
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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