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Molecular Science of Fluctuations Toward Biological Functions pp 125–150Cite as

Unfoldomes and Unfoldomics: Introducing Intrinsically Disordered Proteins

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Abstract

The last decade and a half has witnessed the fall of one of the major paradigms in structural biology. Contrary to the more than a hundred year-old belief that unique protein function is defined by unique crystal-like protein structure which is encoded in unique amino acid sequence, many biologically active proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) are very different from ordered proteins and domains at the variety of levels, starting from the specific and well-recognizable amino acid composition and sequence biases and ending with engagement in biological functions non-accessible to entities with unique and fixed structures. IDPs/IDPRs are highly abundant in nature, and many of them are associated with various human diseases. The functional repertoire of IDPs complements the functions of ordered proteins, with IDPs being often involved in regulation, signaling, and control. Due to their exceptional commonness within the protein universe, combined with a set of specific structural and conformational features, and broad and unique functional repertoire, IDPs and hybrid proteins possessing ordered domains and functional IDPRs clearly comprise unfoldomes within all known proteomes. This chapter provides a brief description of IDPs/IDPRs and shows the place of these exceptionally interesting creatures within the protein kingdom.

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Acknowledgments

This review would not be possible without many colleagues who, over the years, contributed to the introduction and development of the IDP field. Numerous very helpful and thought-promoting discussions with our colleagues and friends are deeply acknowledged.

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Authors and Affiliations

  1. Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd, MDC07, Tampa, FL, 33612, USA

    Bin Xue & Vladimir N. Uversky

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

    Vladimir N. Uversky

  3. Biology Department, Faculty of Science, King Abdulaziz University, 80203, Jeddah, 21589, Kingdom of Saudi Arabia

    Vladimir N. Uversky

  4. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russian Federation

    Vladimir N. Uversky

Authors
  1. Bin Xue
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  2. Vladimir N. Uversky
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Correspondence to Vladimir N. Uversky .

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Editors and Affiliations

  1. Kyoto University, Kyoto, Japan

    Masahide Terazima

  2. Nara Institute of Science and Tech, Ikoma, Japan

    Mikio Kataoka

  3. Sojo University, Kumamoto, Japan

    Ryuichi Ueoka

  4. Nagoya University, Nagoya, Japan

    Yuko Okamoto

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Xue, B., Uversky, V.N. (2016). Unfoldomes and Unfoldomics: Introducing Intrinsically Disordered Proteins. In: Terazima, M., Kataoka, M., Ueoka, R., Okamoto, Y. (eds) Molecular Science of Fluctuations Toward Biological Functions . Springer, Tokyo. https://doi.org/10.1007/978-4-431-55840-8_6

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