The Protein Journal

, Volume 28, Issue 7, pp 305–325

Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding

Article

DOI: 10.1007/s10930-009-9201-4

Cite this article as:
Uversky, V.N. Protein J (2009) 28: 305. doi:10.1007/s10930-009-9201-4

Abstract

Intrinsically disordered proteins (IDPs) differ from “normal” ordered proteins at several levels, structural, functional and conformational. Amino acid biases characteristic for IDPs determine their structural variability and lack of rigid well-folded structure. This structural plasticity is necessary for the unique functional repertoire of IDPs, which is complementary to the catalytic activities of ordered proteins. Amino acid biases also drive atypical responses of IDPs to changes in their environment. The conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack thereof) of the denaturant-induced unfolding, lack of the measurable excess heat absorption peak(s) characteristic for the melting of ordered proteins, “turned out” response to heat and changes in pH, the ability to gain structure in the presence of various counter ions, osmolytes, membranes and binding partners, and by the unique response to macromolecular crowding. This review describes some of the most characteristic features of the IDP conformational behavior and the unique response of IDPs to changes in their environment.

Keywords

Intrinsically disordered proteinIntrinsic disorderConformational behaviorPartially folded conformationMacromolecular crowdingProtein–protein interactionProtein unfoldingOsmolyte

Abbreviations

ANS

8-Anilinonaphthalene-1-sulfonate

CD

Circular dichroism

GdmCl

Guanidinium chloride

ID

Intrinsic disorder

IDP

Intrinsically disordered protein

IDR

Intrinsically disordered region

LUV

Large unilamellar vesicle

PA

1,2-Dipalmitoyl-sn-glycero-3-phosphate

PC

1,2-Dipalmitoyl-sn-glycero-3-phosphocholine

PG

1,2-Dipalmitoyl-sn-glycero-3-phospho-RAC-(1-glycerol

SUV

Small unilamellar vesicle

TMAO

Trimethylamine-N-oxide

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Institute for Intrinsically Disordered Protein Research, The Center for Computational Biology and Bioinformatics, and The Department of Biochemistry and Molecular BiologyIndiana University School of MedicineIndianapolisUSA
  2. 2.Institute for Biological InstrumentationRussian Academy of SciencesPushchino, Moscow RegionRussia