基本信息
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职业迁徙
个人简介
Research
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.
研究兴趣
论文共 70 篇作者统计合作学者相似作者
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Current opinion in structural biology (2023): 102705-102705
biorxiv(2022)
Biomoleculesno. 11 (2022)
SSRN Electronic Journal (2022)
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