Abstract
Protein conformational changes play a critical role in biological functions such as ligand-protein and protein-protein interactions. Due to the noise in structural data, determining salient conformational changes reliably and efficiently is a challenging problem. This paper presents an efficient algorithm for analyzing protein conformational changes, using noisy data. It applies a statistical flexibility test to all contiguous fragments of a protein and combines the information from these tests to compute a consensus flexibility measure for each residue of the protein. We tested the algorithm, using data from the Protein Data Bank and the Macromolecular Movements Database. The results show that our algorithm can reliably detect different types of salient conformational changes, including well-known examples such as hinge well as the flap motion of HIV-1 proteaseThe software implementing software implementing our algorithm is available at http://motion.comp.nus.edu.sg/projects/proflexana/proflexana.html .
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Nigham, A., Hsu, D. (2007). Protein Conformational Flexibility Analysis with Noisy Data. In: Speed, T., Huang, H. (eds) Research in Computational Molecular Biology. RECOMB 2007. Lecture Notes in Computer Science(), vol 4453. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-71681-5_28
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DOI: https://doi.org/10.1007/978-3-540-71681-5_28
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