Ensembles from ordered and disordered proteins reveal similar structural constraints during evolution

MARCHETTI, JULIA; MONZON, ALEXANDER MIGUEL; TOSATTO, SILVIO C. E.; GUSTAVO PARISI; FORNASARI, MARÍA SILVINA

JOURNAL OF MOLECULAR BIOLOGY

ACADEMIC PRESS LTD-ELSEVIER SCIENCE LTD

Lugar: Amsterdam; Año: 2019

0022-2836

The conformations accessible to proteins are determined by the inter-residue interactions between amino acidresidues. During evolution, structural constraints that are required for protein function providing biologicallyrelevant information can exist. Here, we studied the proportion of sites evolving under structural constraintsin two very different types of ensembles, those coming from ordered and disordered proteins. Using astructurally 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 indisordered regions and ~ 57% of them show long-range inter-residue contacts. Also, we found that disorderedensembles are redundant in reference to their structurally constrained evolutionary information and could bedescribed on average with ~ 11 conformers. Despite the different complexity of the studied ensembles andproteins, the similar constraints reveal a comparable level of selective pressure to maintain their biologicalfunctions. These results highlight the importance of the evolutionary information to recover meaningfulbiological information to further characterize conformational ensembles