Revealing the molecular structures of sugars using galectin-10 protein crystals
A quick, purification-free method was developed by researchers at the Institute of Science Tokyo, to capture the detailed 3D structures of flexible sugar molecules. By growing crystals of galectin-10 protein using a cell-free crystallization process and soaking them in sugar solution, the researchers were able to trap and analyze the molecular arrangement of sugars and their interactions with the protein. This offers a powerful tool to accelerate research in drug discovery and molecular biology.
Sugars, or saccharides, do much more than sweeten food. In living organisms, these molecules decorate the surfaces of cells and also act as vital messengers in processes such as infection control and tissue repair.
Understanding how these sugar molecules fold, move, and interact with proteins is important for interpreting their roles. But structural complexity and flexibility make them difficult to study using conventional techniques.
To overcome this challenge, a research team at the Institute of Science Tokyo (Science Tokyo), Japan, led by Professor Takafumi Ueno from the School of Life Science and Technology developed a rapid, purification-free method for structural analysis of sugars.
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