The interplay between structure and function in intrinsically unstructured proteins
Institute of Molecular Life Sciences · Hungarian Academy of Sciences
Abstract
Intrinsically unstructured proteins (IUPs) are common in various proteomes and occupy a unique structural and functional niche in which function is directly linked to structural disorder. The evidence that these proteins exist without a well-defined folded structure in vitro is compelling, and justifies considering them a separate class within the protein world. In this paper, novel advances in the rapidly advancing field of IUPs are reviewed, with the major attention directed to the evidence of their unfolded character in vivo, the interplay of their residual structure and their various functional modes and the functional benefits their malleable structural state provides. Via all these details, it is…
Citation impact
- FWCI
- 16.17
- Percentile
- 100%
- References
- 84
Authors
1Topics & keywords
- Intrinsically disordered proteins
- Computational biology
- Function (biology)
- Protein structure
- Proteome
- Protein folding
- Chemistry
- Biology