Intrinsically unstructured proteins

Trends Biochem Sci. 2002 Oct;27(10):527-33. doi: 10.1016/s0968-0004(02)02169-2.


The recent suggestion that the classical structure-function paradigm should be extended to proteins and protein domains whose native and functional state is intrinsically unstructured has received a great deal of support. There is ample evidence that the unstructured state, common to all living organisms, is essential for basic cellular functions; thus it deserves to be recognized as a separate functional and structural category within the protein kingdom. In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where these proteins can be comprehensively classified on the basis of structure and function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry
  • Entropy
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding
  • Proteins / chemistry*
  • Proteins / classification*
  • Proteins / metabolism
  • Static Electricity
  • Structure-Activity Relationship


  • Amino Acids
  • Proteins