Abstract
Plasmodium vivax Merozoite Surface Protein-3α and 3β 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 α-helical secondary and coiled-coil tertiary structures. Seven recombinant proteins representing different regions of MSP-3α and MSP-3β of P. vivax were generated to investigate their structure . Circular dichroism spectra analysis revealed that some proteins are folded with a high degree of α-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-3α, 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
