期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 431, 期 6, 页码 1298-1307出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.01.031
关键词
protein evolution; protein ensemble; conformational diversity; disordered proteins
资金
- Universidad Nacional de Quilmes [PUNQ 1004/11]
- Agencia de Ciencia y Tecnologia [PICT-2014-3430]
- COST Action [BM1405]
- European Union [778247]
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, similar to 68% are in disordered regions and similar to 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 similar to 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. (C) 2019 Elsevier Ltd. All rights reserved.
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