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A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon’s Information Theory

1
Department of Computer Science and Engineering, SimCenter, University of Tennessee, Chattanooga, TN 37403, USA
2
Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA
3
Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA
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Department of Biology, Geology, and Environmental Science, University of Tennessee, Chattanooga, TN 37403, USA
*
Authors to whom correspondence should be addressed.
Entropy 2019, 21(6), 591; https://doi.org/10.3390/e21060591
Received: 27 April 2019 / Revised: 11 June 2019 / Accepted: 13 June 2019 / Published: 14 June 2019
We propose a framework to convert the protein intrinsic disorder content to structural entropy (H) using Shannon’s information theory (IT). The structural capacity (C), which is the sum of H and structural information (I), is equal to the amino acid sequence length of the protein. The structural entropy of the residues expands a continuous spectrum, ranging from 0 (fully ordered) to 1 (fully disordered), consistent with Shannon’s IT, which scores the fully-determined state 0 and the fully-uncertain state 1. The intrinsically disordered proteins (IDPs) in a living cell may participate in maintaining the high-energy-low-entropy state. In addition, under this framework, the biological functions performed by proteins and associated with the order or disorder of their 3D structures could be explained in terms of information-gains or entropy-losses, or the reverse processes. View Full-Text
Keywords: intrinsically disordered proteins; entropy; information intrinsically disordered proteins; entropy; information
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Guo, H.-B.; Ma, Y.; Tuskan, G.A.; Qin, H.; Yang, X.; Guo, H. A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon’s Information Theory. Entropy 2019, 21, 591.

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