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Intrinsically disordered protein.

A K Dunker1, J D Lawson, C J Brown

  • 1School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4660, USA. dunker@mail.wsu.edu

Journal of Molecular Graphics & Modelling
|May 31, 2001
PubMed
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Native proteins can adopt ordered, molten globule, or random coil structures, with function arising from any state. This intrinsic protein disorder is more prevalent than previously thought, especially in eukaryotes.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Genomics

Background:

  • Proteins exist in ordered, molten globule, or random coil states.
  • Native protein structure and function can arise from any of these states, including transitions between them.
  • Examples like fd phage, nucleosomes, clusterin, calcineurin, and calsequestrin illustrate proteins functioning in non-ordered states.

Purpose of the Study:

  • To demonstrate that native protein structure and function can originate from ordered, molten globule, or random coil states.
  • To highlight the prevalence and functional significance of intrinsic protein disorder.
  • To investigate the relationship between amino acid sequence and protein order/disorder.

Main Methods:

  • Analysis of existing literature and examples of protein structures and functions.

Related Experiment Videos

  • Investigation of specific protein systems (fd phage, nucleosomes, clusterin, calcineurin, calsequestrin).
  • Computational prediction of intrinsic protein disorder from amino acid sequences.

    • Main Results:

    • Native protein structure and function are not limited to the ordered state; molten globules and random coils also play crucial roles.
    • Intrinsic protein disorder is a common feature, with disordered regions serving diverse functions (e.g., molecular recognition, flexible linkers).
    • Disorder is an encoded property of amino acid sequences, and predictions suggest significantly more disordered proteins exist than are represented in the Protein Data Bank.

    Conclusions:

    • Protein structure and function are more diverse than traditionally assumed, encompassing ordered, molten globule, and disordered states.
    • Intrinsic protein disorder is a significant and encoded feature of proteins, particularly prevalent in eukaryotes.
    • Future research should focus on understanding the sequence-disorder relationship for accurate prediction and characterization of protein function.