Associate Professor of Physics
My research involves the structural analysis of macromolecules by X-ray diffraction. Such studies provide direct and unambiguous information regarding all the details of the three-dimentional atomic arrangement of these molecules. This information is necessary in order to understand their properties and function.
My current efforts focus in acquiring a better understanding of de novo pyrimidine biosynthesis at the molecular level. In this connection, I have determined the structure of the catalytic trimer of the enzyme Aspartate transcarbamoylase from the hyperthermophilic and barophilic archaeon M.jannaschii in two crystal forms. This research gave insight into the strategies for thermostabilization of this important enzyme. The most intriguing feature of these structures is the association of crystallographically independent subunits in pairs into a novel staggered complex with a short inter-trimer distance of 33.8 Å. This novel staggered arrangement may be present in the holoenzyme in vivo in the presence of the regulatory subunits. In order to gain more insight into the mechanism of catalysis we co-crystallize the enzyme with substrate analogs.
Past research includes complexes of bovine thrombin with inhibitors including the leech protein hirudin, one Fab fragment, S100b, the EF-Tu-Ts complex, pectin lyase B, histidine decarboxylase, the Gly121Tyr mutant of ornithine decarboxylase from Lactobacillus 30a, the UP1 fragment of hnRNP A1, myoglobin, and insulin.
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My current efforts focus in acquiring a better understanding of de novo pyrimidine biosynthesis at the molecular level. In this connection, I have determined the structure of the catalytic trimer of the enzyme Aspartate transcarbamoylase from the hyperthermophilic and barophilic archaeon M.jannaschii in two crystal forms. This research gave insight into the strategies for thermostabilization of this important enzyme. The most intriguing feature of these structures is the association of crystallographically independent subunits in pairs into a novel staggered complex with a short inter-trimer distance of 33.8 Å. This novel staggered arrangement may be present in the holoenzyme in vivo in the presence of the regulatory subunits. In order to gain more insight into the mechanism of catalysis we co-crystallize the enzyme with substrate analogs.
Past research includes complexes of bovine thrombin with inhibitors including the leech protein hirudin, one Fab fragment, S100b, the EF-Tu-Ts complex, pectin lyase B, histidine decarboxylase, the Gly121Tyr mutant of ornithine decarboxylase from Lactobacillus 30a, the UP1 fragment of hnRNP A1, myoglobin, and insulin.
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About Jacqueline Vitali
My research involves the structural analysis of macromolecules by X-ray diffraction. Such studies provide direct and unambiguous information regarding all the details of the three-dimentional atomic arrangement of these molecules. This information is necessary in order to understand their properties and function.
My current efforts focus in acquiring a better understanding of de novo pyrimidine biosynthesis at the molecular level. In this connection, I have determined the structure of the catalytic trimer of the enzyme Aspartate transcarbamoylase from the hyperthermophilic and barophilic archaeon M.jannaschii in two crystal forms. This research gave insight into the strategies for thermostabilization of this important enzyme. The most intriguing feature of these structures is the association of crystallographically independent subunits in pairs into a novel staggered complex with a short inter-trimer distance of 33.8 Å. This novel staggered arrangement may be present in the holoenzyme in vivo in the presence of the regulatory subunits. In order to gain more insight into the mechanism of catalysis we co-crystallize the enzyme with substrate analogs.
Past research includes complexes of bovine thrombin with inhibitors including the leech protein hirudin, one Fab fragment, S100b, the EF-Tu-Ts complex, pectin lyase B, histidine decarboxylase, the Gly121Tyr mutant of ornithine decarboxylase from Lactobacillus 30a, the UP1 fragment of hnRNP A1, myoglobin, and insulin.
My current efforts focus in acquiring a better understanding of de novo pyrimidine biosynthesis at the molecular level. In this connection, I have determined the structure of the catalytic trimer of the enzyme Aspartate transcarbamoylase from the hyperthermophilic and barophilic archaeon M.jannaschii in two crystal forms. This research gave insight into the strategies for thermostabilization of this important enzyme. The most intriguing feature of these structures is the association of crystallographically independent subunits in pairs into a novel staggered complex with a short inter-trimer distance of 33.8 Å. This novel staggered arrangement may be present in the holoenzyme in vivo in the presence of the regulatory subunits. In order to gain more insight into the mechanism of catalysis we co-crystallize the enzyme with substrate analogs.
Past research includes complexes of bovine thrombin with inhibitors including the leech protein hirudin, one Fab fragment, S100b, the EF-Tu-Ts complex, pectin lyase B, histidine decarboxylase, the Gly121Tyr mutant of ornithine decarboxylase from Lactobacillus 30a, the UP1 fragment of hnRNP A1, myoglobin, and insulin.
| Present | Associate Professor of Physics, Cleveland State University | |
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Disciplines
Contact Information
Office: SI 122
Phone: 216-687-2431
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