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• W3156336811 abstract "To understand how proteins function on a cellular level, it is of paramount importance to understand their structures and dynamics, including the conformational changes they undergo to carry out their function. For the aforementioned reasons, the study of large conformational changes in proteins has been an interest to researchers for years. However, since some proteins experience rapid and transient conformational changes, it is hard to experimentally capture the intermediate structures. Additionally, computational brute force methods are computationally intractable, which makes it impossible to find these pathways which require a search in a high-dimensional, complex space. In our previous work, we implemented a hybrid algorithm that combines Monte-Carlo (MC) sampling and RRT*, a version of the Rapidly Exploring Random Trees (RRT) robotics-based method, to make the conformational exploration more accurate and efficient, and produce smooth conformational pathways. In this work, we integrated the rigidity analysis of proteins into our algorithm to guide the search to explore flexible regions. We demonstrate that rigidity analysis dramatically reduces the run time and accelerates convergence." @default.
• W3156336811 created "2021-04-26" @default.
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• W3156336811 date "2021-04-16" @default.
• W3156336811 modified "2023-09-25" @default.
• W3156336811 title "Integrating Rigidity Analysis into the Exploration of Protein Conformational Pathways Using RRT* and MC" @default.
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• W3156336811 doi "https://doi.org/10.3390/molecules26082329" @default.
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