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Target recognition and expression mechanism of intrinsically disordered protein

Intrinsically disordered proteins (IDPs) are characterized by a lack of stable tertiary structure when they exist as isolated polypeptide chains under physiological conditions. Their folding is coupled to binding, so that they adopt well-defined structures upon interacting with their targets. This novel partner protein recognition mechanism is unlike the well-known "lock and key" and induced-fit models. IDPs are mostly found in eukaryotes, and generally interact with several target proteins, playing important roles as hubs in intracellular networks. In this research project, scientists in the fields of structural biology, molecular biology and bioinformatics are working together to analyze the structures and properties of IDPs-how they find, bind, and fold with their partners, and carry out different functions. This new project that we are establishing blends physics, chemistry and biology together into a new interdisciplinary research area.

Head Investigator: Mamoru Sato
Professor of Graduate School of Nanobioscience, Yokohama City University

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