Abstract
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.
Original language | English |
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Article number | 591 |
Journal | Entropy |
Volume | 21 |
Issue number | 6 |
DOIs | |
State | Published - Jun 1 2019 |
Funding
Acknowledgments: This work is supported by the Department of Energy (DOE), Office of Science, Genomic Science Program under Award Number DE-SC0008834. Oak Ridge National Laboratory is managed by UT-Battelle, LLC for the US DOE, under Contract Number DE-AC05-00OR22725. HBG and HQ acknowledge the support of NSF Career award #1453078 (transferred to #1720215), BD Spoke #1761839, and internal funding of University of Tennessee at Chattanooga. We thank three anonymous reviewers for providing valuable suggestions to our manuscript. We acknowledge Bailey Kirby for a thorough proofreading of the manuscript.
Keywords
- Entropy
- Information
- Intrinsically disordered proteins