期刊
PROTEIN SCIENCE
卷 25, 期 6, 页码 1138-1146出版社
WILEY
DOI: 10.1002/pro.2931
关键词
disorder; conformational diversity; protein function; transitions
资金
- COST Action [BM1405]
- UNQ
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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