Ensembles from Ordered and Disordered Proteins Reveal Similar Structural Constraints during Evolution |
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| Institution: | 1. Departamento de Ciencia y Tecnología, CONICET, Universidad Nacional de Quilmes, Roque Sáenz Peña 352, B1876BXD, Bernal, Provincia de Buenos Aires, Argentina;2. Department of Biomedical Sciences, University of Padua, Padua, Italy;1. Department of Chemistry and Biochemistry, and Center for One Health Studies, Berry College, Mt. Berry, GA 30149, USA;2. Department of Chemistry and Biochemistry, Center for RNA Biology, and Center for Retrovirus Research, Ohio State University, Columbus, OH 43210, USA;1. Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 3E1, Canada;2. Donnelly Centre for Cellular and Biomolecular Research, Banting and Best Department of Medical Research, University of Toronto, Toronto, ON, M5S3E1, Canada;3. Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada;4. Lunenfeld–Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, ON M5G 1X5, Canada;5. Boston Biochem, a Bio-Techne Brand 840 Memorial Drive, Cambridge, MA 02139, USA;6. Canadian Institute for Advanced Research, Toronto, ON, M5G1Z8, Canada;1. Department of Biology, University of Copenhagen, Ole Maaløes vej 5, DK-2200 Copenhagen N, Denmark;2. Center for Models of Life, Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, DK-2100 Copenhagen Ø, Denmark;1. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, PR China;2. State Key Laboratory of Ocean Engineering, School of Naval Architecture, Ocean and Civil Engineering, Shanghai Jiao Tong University, Shanghai 200240, PR China;3. Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, PR China;4. Department of Pharmacology and Chemical Biology, Institute of Medical Sciences, School of Medicine, Shanghai Jiao Tong University, Shanghai 200025, PR China |
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| Abstract: | The conformations accessible to proteins are determined by the inter-residue interactions between amino acid residues. During evolution, structural constraints that are required for protein function providing biologically relevant information can exist. Here, we studied the proportion of sites evolving under structural constraints in two very different types of ensembles, those coming from ordered and disordered proteins. Using a structurally constrained model of protein evolution, we found that both types of ensembles show comparable, near 40%, number of positions evolving under structural constraints. Among these sites, ~ 68% are in disordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disordered ensembles are redundant in reference to their structurally constrained evolutionary information and could be described on average with ~ 11 conformers. Despite the different complexity of the studied ensembles and proteins, the similar constraints reveal a comparable level of selective pressure to maintain their biological functions. These results highlight the importance of the evolutionary information to recover meaningful biological information to further characterize conformational ensembles. |
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