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| Name |
Gronenborn, Angela M. |
| Location
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University of Pittsburgh School of Medicine |
| Primary Field
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Biophysics and Computational Biology |
| Secondary Field
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Chemistry |
 Election Citation
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Gronenborn pioneered the development of NMR spectroscopy for determining three-dimensional structures of biological macromolecules in solution. Her lab investigates cellular processes at the molecular and atomic levels in relation to human disease, such as HIV pathogenesis, and has found that a small number of conservative mutations can impact protein fold, domain swapping, and fibril formation. |
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Research Interests
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Our laboratory combines NMR spectroscopy with Biophysics, Biochemistry, and Chemistry to investigate cellular processes at the molecular and atomic levels in relation to human disease. We presently focus on two areas in biology: Gene Regulation and HIV pathogenesis. In order to understand how biological macromolecules work and to intervene in a rational manner with respect to activity and function, detailed knowledge of their architecture and dynamic features is required. Evaluation of the major determinants for stability and conformational specificity of normal and disease-causing forms of such proteins allows us to unravel complex disease processes. |
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