Structure and Function of Biological Macromolecules and Complexes
The main focus of our research is to resolve and understand the structure of membrane and membrane-associated proteins and complexes combining cryo-electron microscopy (Cryo-EM), molecular biophysics and molecular modeling.
Cryo-electron microscopy (Cryo-EM) and crystallography is a powerful method to study the structure, assembly, and dynamics of biological macromolecules and their interactions in close to native conditions and subnanometer resolution. Cryo-EM is capable of visualizing fully hydrated lipid structures, as lipid bilayer and phases at atomic resolution. Thus protein-protein and protein-membrane interactions can be followed at a molecular level and their structure resolved in close to native environment.
We have great interest and experience in defining the membrane-bound structure of coagulation Factors VIII and V and their complexes with the respective proteases: Factors IXa and Xa by Cryo-EM. Our main goal is to generate functional models of these important for coagulation macromolecular assemblies. For this purpose we have developed lipid nanoplatforms such as: single bilayer lipid nanotubes (LNT), lipid nanodisks (LND) and vesicles, which facilitate the functional structure determination of these proteins and complexes by Cryo-EM at closest to physiological conditions.
Cryo-electron microscopy (Cryo-EM) and crystallography is a powerful method to study the structure, assembly, and dynamics of biological macromolecules and their interactions in close to native conditions and subnanometer resolution. Cryo-EM is capable of visualizing fully hydrated lipid structures, as lipid bilayer and phases at atomic resolution. Thus protein-protein and protein-membrane interactions can be followed at a molecular level and their structure resolved in close to native environment.
We have great interest and experience in defining the membrane-bound structure of coagulation Factors VIII and V and their complexes with the respective proteases: Factors IXa and Xa by Cryo-EM. Our main goal is to generate functional models of these important for coagulation macromolecular assemblies. For this purpose we have developed lipid nanoplatforms such as: single bilayer lipid nanotubes (LNT), lipid nanodisks (LND) and vesicles, which facilitate the functional structure determination of these proteins and complexes by Cryo-EM at closest to physiological conditions.
The ultimate goal of our research is to develop and combine our knowledge of the membrane-bound organization of blood coagulation factors and complexes with the nano-technology expertise in our laboratory to propose novel and effective pharmaceutical interventions against hemophilia and thrombosis.
We are further including single particle Cryo-EM and Cryo-electron tomography approaches to our research, to gain more information on the macromolecular assemblies we study and answer biologically relevant questions.
We are further including single particle Cryo-EM and Cryo-electron tomography approaches to our research, to gain more information on the macromolecular assemblies we study and answer biologically relevant questions.
Svetla Stoilova-McPhie, Ph.D.
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University of Texas Medical Branch
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