Unknown

Dataset Information

0

Physicochemical classification of organisms.


ABSTRACT: The hypervariable residues that compose the major part of proteins’ surfaces are generally considered outside evolutionary control. Yet, these “nonconserved” residues determine the outcome of stochastic encounters in crowded cells. It has recently become apparent that these encounters are not as random as one might imagine, but carefully orchestrated by the intracellular electrostatics to optimize protein diffusion, interactivity, and partner search. The most influential factor here is the protein surface-charge density, which takes different optimal values across organisms with different intracellular conditions. In this study, we examine how far the net-charge density and other physicochemical properties of proteomes will take us in terms of distinguishing organisms in general. The results show that these global proteome properties not only follow the established taxonomical hierarchy, but also provide clues to functional adaptation. In many cases, the proteome–property divergence is even resolved at species level. Accordingly, the variable parts of the genes are not as free to drift as they seem in sequence alignment, but present a complementary tool for functional, taxonomic, and evolutionary assignment.

SUBMITTER: Vallina Estrada E 

PROVIDER: S-EPMC9171632 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Physicochemical classification of organisms.

Vallina Estrada Eloy E   Oliveberg Mikael M  

Proceedings of the National Academy of Sciences of the United States of America 20220502 19


The hypervariable residues that compose the major part of proteins’ surfaces are generally considered outside evolutionary control. Yet, these “nonconserved” residues determine the outcome of stochastic encounters in crowded cells. It has recently become apparent that these encounters are not as random as one might imagine, but carefully orchestrated by the intracellular electrostatics to optimize protein diffusion, interactivity, and partner search. The most influential factor here is the prote  ...[more]

Similar Datasets

| S-EPMC4418965 | biostudies-literature
| S-EPMC6699418 | biostudies-literature
| S-EPMC5704239 | biostudies-literature
| S-EPMC5159126 | biostudies-literature
| S-EPMC2876039 | biostudies-literature
| S-EPMC196707 | biostudies-other
| S-EPMC6282327 | biostudies-literature
| S-EPMC8351319 | biostudies-literature
| S-EPMC2951700 | biostudies-literature
| S-EPMC6104016 | biostudies-literature