| Structure of macromolecular assemblies |
RESEARCH SUMMARY
The analysis of different viral particles related to the morphogenesis of bacteriophage T7 has allowed us to obtain detailed information of the structural changes involved in the maturation of the viral shell, including a reorganization of the domains of the shell protein, as well as a drastic change in the portal-core complex and its interaction with the shell. We are presently improving the resolution of these viral particles to map the aminoacids involved in these structural transitions.
On the other hand, we are working in the characterization of nano-mechanical properties of these macromolecular containers by atomic force microscopy (AFM). These studies are framed within a collaboration with the group of Dr. J.M. Valpuesta to implement techniques for single molecule analysis using AFM and optical tweezers. Furthermore, we are developing electron tomography methods for the study of large macromolecular aggregates without any symmetry, as well as for their analysis within the cellular environment at improved resolution.
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The activity of the group is focused in the study of macromolecular nanomachines that carry out defined biological functions. Among other systems, we are studying the molecular bases of assembly and maturation in viral systems. To this end we integrate different approaches, as the controlled production of structural components, as well as their structural, functional and nano-mechanical characterization.
The resolution of the T7 connector complex at 0,8 nm has shown the existence of a general domain in viral connectors that might play a fundamental role in DNA translocation.