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Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins

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Book cover Intrinsically Disordered Protein Analysis

Part of the book series: Methods in Molecular Biology ((MIMB,volume 896))

Abstract

Intrinsically disordered proteins (IDPs) differ from ordered proteins at several levels: structural, functional, and conformational. Amino acid biases also drive atypical responses of IDPs to changes in their environment. Among several specific features, the conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack thereof) of the denaturant-induced unfolding. In fact, the denaturant-induced unfolding of native molten globules can be described by shallow sigmoidal curves, whereas urea- or guanidinium hydrochloride-induced unfolding of native pre-molten globules or native coils is a noncooperative process and typically is seen as monotonous feature-less changes in the studied parameters. This chapter describes some of the most characteristic features of the IDP conformational behavior.

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Author information

Authors and Affiliations

  1. Dipartimento di Biochimica “G. Moruzzi”, Università di Bologna, Via San Donato, Bologna, Italy

    Paolo Neyroz

  2. Department of Agro-Environmental Science and Technology, University of Bologna, Bologna, Italy

    Stefano Ciurli

  3. Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, FL, USA

    Vladimir N. Uversky

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

    Vladimir N. Uversky

Authors
  1. Paolo Neyroz
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  2. Stefano Ciurli
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  3. Vladimir N. Uversky
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Corresponding authors

Correspondence to Stefano Ciurli or Vladimir N. Uversky .

Editor information

Editors and Affiliations

  1. DEPT OF MOLECULAR MED, College of Medicine, University of South Florida, BRUCE B DOWNS BLVD 12901, TAMPA, 33612, Florida, USA

    Vladimir N. Uversky

  2. Dept. Biochemistry & Molecular Biology, Center for Computational Biology &, Indiana University, West 10th Street 410, Indianapolis, 46202, Indiana, USA

    A. Keith Dunker

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Neyroz, P., Ciurli, S., Uversky, V.N. (2012). Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 896. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3704-8_12

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  • DOI: https://doi.org/10.1007/978-1-4614-3704-8_12

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