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Research in my group is focused on identifying fundamental relationships between protein structure and function. We are particularly interested in proteins, like the tumor suppressor p53, that are involved in the development and maintenance of cancer. p53 is a tumor suppressor and cell cycle regulator that is activated by protein-protein interactions and posttranslational modifications (PTMs). Deletion or mutation of p53 can dramatically increase susceptibility to cancer. p53 is also an intrinsically disordered protein (IDP). IDPs are highly dynamic, do not form stable tertiary structures, and contain variable amounts of transient secondary structure. IDP domains are hotspots for PTMs and they frequently mediate protein-protein interactions through coupled folding and binding. IDP domains that interact with other proteins can contain defined levels of transient secondary structure that resemble their complex-bound structure. These levels of residual structure can modulate binding affinities with other proteins by tuning the change in conformational entropy that occurs during the coupled folding and binding reaction.
Research in my group is focused on identifying fundamental relationships between protein structure and function. We are particularly interested in proteins, like the tumor suppressor p53, that are involved in the development and maintenance of cancer. p53 is a tumor suppressor and cell cycle regulator that is activated by protein-protein interactions and posttranslational modifications (PTMs). Deletion or mutation of p53 can dramatically increase susceptibility to cancer. p53 is also an intrinsically disordered protein (IDP). IDPs are highly dynamic, do not form stable tertiary structures, and contain variable amounts of transient secondary structure. IDP domains are hotspots for PTMs and they frequently mediate protein-protein interactions through coupled folding and binding. IDP domains that interact with other proteins can contain defined levels of transient secondary structure that resemble their complex-bound structure. These levels of residual structure can modulate binding affinities with other proteins by tuning the change in conformational entropy that occurs during the coupled folding and binding reaction.
Research Interests
Papers共 78 篇Author StatisticsCo-AuthorSimilar Experts
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Current opinion in structural biology (2023): 102705-102705
Nature Structural & Molecular Biologyno. 8 (2022): 781-790
BIOMOLECULESno. 11 (2022): 1558-1558
SSRN Electronic Journal (2022)
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