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Disorder transitions and conformational diversity cooperatively modulate biological function in proteins
Author(s) -
Zea Diego Javier,
Monzon Alexander Miguel,
Gonzalez Claudia,
Fornasari María Silvina,
Tosatto Silvio C. E.,
Parisi Gustavo
Publication year - 2016
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2931
Subject(s) - conformational isomerism , intrinsically disordered proteins , function (biology) , protein structure , conformational change , chemistry , functional diversity , diversity (politics) , biophysics , crystallography , stereochemistry , biology , molecule , biochemistry , evolutionary biology , ecology , organic chemistry , sociology , anthropology
Structural differences between conformers sustain protein biological function. Here, we studied in a large dataset of 745 intrinsically disordered proteins, how ordered‐disordered transitions modulate structural differences between conformers as derived from crystallographic data. We found that almost 50% of the proteins studied show no transitions and have low conformational diversity while the rest show transitions and a higher conformational diversity. In this last subset, 60% of the proteins become more ordered after ligand binding, while 40% more disordered. As protein conformational diversity is inherently connected with protein function our analysis suggests differences in structure‐function relationships related to order‐disorder transitions.

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