reviewFEBS LettersApr 8, 2005Closed access

The interplay between structure and function in intrinsically unstructured proteins

Institute of Molecular Life Sciences · Hungarian Academy of Sciences

PubMed
Indexed incrossrefpubmed

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

710
total citations
FWCI
16.17
Percentile
100%
References
84
Citations per year

Authors

1

Topics & keywords

Keywords
  • Intrinsically disordered proteins
  • Computational biology
  • Function (biology)
  • Protein structure
  • Proteome
  • Protein folding
  • Chemistry
  • Biology
No related works found for this paper.