Biophysical characterization of the recombinant merozoite surface protein-3 of Plasmodium vivax
| Autor: | Carlos H.I. Ramos, Maria Carolina Sarti Jimenez, John W. Barnwell, Mauricio M. Rodrigues, Irene S. Soares, Mary R. Galinski, João Alexandre Ribeiro Gonçalves Barbosa |
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| Rok vydání: | 2008 |
| Předmět: |
Circular dichroism
Recombinant Fusion Proteins Plasmodium vivax Biophysics Protozoan Proteins Antigens Protozoan Biology Biochemistry Protein Structure Secondary law.invention Protein structure law parasitic diseases Animals Merozoite surface protein Molecular Biology Protein secondary structure Alanine Molecular mass Circular Dichroism biology.organism_classification Random coil Protein Structure Tertiary Crystallography Recombinant DNA Plasmids |
| Zdroj: | Biochimica et biophysica acta. 1780(7-8) |
| ISSN: | 0006-3002 |
| Popis: | Plasmodium vivax Merozoite Surface Protein-3alpha and 3beta 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-3alpha and MSP-3beta 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-3alpha, 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. |
| Databáze: | OpenAIRE |
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