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

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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.

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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

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Acknowledgments

I am grateful to Prof. Keith A. Dunker for numerous valuable discussions and constant support. Many thanks to all of my colleagues and collaborators around the globe for their invaluable contributions to the IDP field. This work was supported in part by the Program of the Russian Academy of Sciences for the “Molecular and cellular biology”, and by grants R01 LM007688-01A1 and GM071714-01A2 from the National Institutes of Health. I gratefully acknowledge the support of the IUPUI Signature Centers Initiative.

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  1. Institute for Intrinsically Disordered Protein Research, The Center for Computational Biology and Bioinformatics, and The Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 410W. 10th Street, HS 5009, Indianapolis, IN, 46202, USA

    Vladimir N. Uversky

  2. Institute for Biological Instrumentation, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    Vladimir N. Uversky

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Correspondence to Vladimir N. Uversky.

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Uversky, V.N. Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding. Protein J 28, 305–325 (2009). https://doi.org/10.1007/s10930-009-9201-4

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