Literature DB >> 26851286

Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.

Vladimir N Uversky1.   

Abstract

Biologically active but floppy proteins represent a new reality of modern protein science. These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and intrinsically disordered protein regions (IDPRs) constitute a noticeable part of any given proteome. Functionally, they complement ordered proteins, and their conformational flexibility and structural plasticity allow them to perform impossible tricks and be engaged in biological activities that are inaccessible to well folded proteins with their unique structures. The major goals of this minireview are to show that, despite their simplified amino acid sequences, IDPs/IDPRs are complex entities often resembling chaotic systems, are structurally and functionally heterogeneous, and can be considered an important part of the structure-function continuum. Furthermore, IDPs/IDPRs are everywhere, and are ubiquitously engaged in various interactions characterized by a wide spectrum of binding scenarios and an even wider spectrum of structural and functional outputs.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Entities:  

Keywords:  complexity; dynamical system; intrinsically disordered protein; intrinsically disordered proteins; multifunctional protein; post-translational modification (PTM); posttranslational modification; protein folding; protein-protein interaction; structural heterogeneity

Mesh:

Substances:

Year:  2016        PMID: 26851286      PMCID: PMC4807255          DOI: 10.1074/jbc.R115.685859

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  95 in total

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Review 5.  What does it mean to be natively unfolded?

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Journal:  Eur J Biochem       Date:  2002-01

Review 6.  Coupling of folding and binding for unstructured proteins.

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Journal:  Curr Opin Struct Biol       Date:  2002-02       Impact factor: 6.809

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Review 9.  Intrinsically disordered protein.

Authors:  A K Dunker; J D Lawson; C J Brown; R M Williams; P Romero; J S Oh; C J Oldfield; A M Campen; C M Ratliff; K W Hipps; J Ausio; M S Nissen; R Reeves; C Kang; C R Kissinger; R W Bailey; M D Griswold; W Chiu; E C Garner; Z Obradovic
Journal:  J Mol Graph Model       Date:  2001       Impact factor: 2.518

10.  Intrinsic protein disorder in complete genomes.

Authors:  A K Dunker; Z Obradovic; P Romero; E C Garner; C J Brown
Journal:  Genome Inform Ser Workshop Genome Inform       Date:  2000
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  63 in total

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Review 2.  The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.

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3.  Intrinsic disorder in spondins and some of their interacting partners.

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4.  Preferential binding effects on protein structure and dynamics revealed by coarse-grained Monte Carlo simulation.

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Journal:  J Bioenerg Biomembr       Date:  2018-09-28       Impact factor: 2.945

7.  Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum.

Authors:  Anna Rita Migliaccio; Vladimir N Uversky
Journal:  J Biomol Struct Dyn       Date:  2017-05-26

8.  Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis.

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9.  Sequence composition versus sequence order in the cryoprotective function of an intrinsically disordered stress-response protein.

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