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Wang Jin, a researcher at the National Key Laboratory of Electroanalytic Chemistry at the Chun Institute of Applied Chemistry of the Chinese Academy of Sciences, and Liu Fei, a doctoral student in the School of Physics of Jilin University, proposed the energy landscape landscape and mechanism of mixing calcitonin with its target in the biomolytic identification process by molecular dynamics simulation, and revealed the important link between this mixing mechanism and calcification protein and multi-specific binding of various targets.
published in the Proceedings of the National Academy of Sciences (PNAS, 114, E3927-E3934, 2017).
calcitonin is a signal protein that binds to more than 300 targets and transmits calcium ion signals to various biological processes, thus achieving various functions such as gene regulation, cell skeleton tissue, muscle contraction, signal transducing, metabolic regulation, etc.
the molecular mechanisms of multisemetric identification of calcitonin and multiple targets are essential to understanding these biological processes.
Wang Jin task force, by constructing a meso-view image transformation model, used molecular dynamics to study the binding process of the local image change of calcium-adjusted protein and the binding of the global structure change of the target.
For the identification process of calcium-toned proteins and binding targets, they found atypical "induced fitting", atypical "image selection" and "simultaneous folding" mixed energy landscape, and revealed the important link between this mixing mechanism and the multi-specific binding of calcium-toned proteins with multiple targets.
further studies have found that this complex mechanism is determined by the coordination of potential interactions between molecules and biomedical flexibility.
Calcitonin's biologically evolved natural structure and its target-specific natural structure will lead to a variety of different but optimal binding options for its binding process, which will eventually lead to high affinity and specificity, which undoubtedly increases the probability of multi-specific binding between biomons.
this study provides a global quantitative physical mechanism for the subject of multisemetric binding of proteins and proteins, and enriches people's understanding of the mutual recognition of biological molecules.
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