Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Biophysical characterization of the recombinant merozoite surface protein-3 of Plasmodium vivax|
|Author:||JIMENEZ, Maria Carolina S.|
RAMOS, Carlos Henrique I.
BARBOSA, Joao Alexandre R. G.
GALINSKI, Mary R.
BARNWELL, John W.
RODRIGUES, Mauricio M.
SOARES, Irene S.
|Abstract:||Plasmodium vivax Merozoite Surface Protein-3 alpha and 3 beta are members of a family of related merozoite surface proteins that contain a central alanine-rich domain with heptad repeats that is predicted to form alpha-helical secondary and coiled-coil tertiary structures. Seven recombinant proteins representing different regions of MSP-3 alpha and MSP-3 beta of P. vivax were generated to investigate their structure. Circular dichroism spectra analysis revealed that some proteins are folded with a high degree of alpha-helices as secondary structure, whereas other products contain a high content of random coil. Using size exclusion chromatography, we found that the two smaller fragments of the MSP-3 alpha, named CC4 and CC5, predicted to form coiled-coil (CC) structures, eluted at volumes corresponding to molecular weights larger than their monomeric masses. This result suggests that both proteins are oligomeric molecules. Analytical ultracentrifugation experiments showed that the CC5 oligomers are elongated molecules. Together, these data may help to understand important aspects of P. vivax biology. (C) 2008 Elsevier B.V. All rights reserved.|
merozoite surface protein-3
|Editor:||ELSEVIER SCIENCE BV|
|Citation:||BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1780, n.7/Ago, p.983-988, 2008|
|Appears in Collections:||IB - Artigos e Outros Documentos|
Files in This Item:
|art_JIMENEZ_Biophysical_characterization_of_the_recombinant_merozoite_surface_2008.pdf||published version||789.01 kB||Adobe PDF||View/Open|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.