Intrinsically disordered proteins

V. N. Uversky, A. K. Dunker

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter introduces intrinsically disordered proteins, which do not have rigid three-dimensional (3-D) structures under physiological conditions, but which nevertheless carry out numerous biological functions. Such proteins challenge the prevailing structure-function paradigm, according to which the unique 3-D structure of a protein is a prerequisite to its function. Here we argue that the prevailing paradigm needs to be expanded to include intrinsically disordered proteins and their new relationships among protein sequence, structure, and function. Since this extended paradigm opens new levels of understanding of the complex life of proteins, it represents a major breakthrough for biochemistry, biophysics, and molecular biology.

Original languageEnglish (US)
Title of host publicationComprehensive Biophysics
PublisherElsevier Inc.
Pages170-211
Number of pages42
Volume3
ISBN (Print)9780080957180
DOIs
StatePublished - Dec 1 2012

Keywords

  • Conformational ensemble
  • Intrinsically disordered protein
  • Intrinsically unstructured protein
  • Natively disordered protein
  • Natively unfolded protein
  • Structure-function paradigm

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Uversky, V. N., & Dunker, A. K. (2012). Intrinsically disordered proteins. In Comprehensive Biophysics (Vol. 3, pp. 170-211). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-374920-8.00312-X