Abstract
The traditional view of the structure-function paradigm is that a protein's function is inextricably linked to a well defined, three-dimensional structure, which is determined by the protein's primary amino acid sequence. However, it is now accepted that a number of proteins do not adopt a unique tertiary structure in solution and that some degree of disorder is required for many proteins to perform their prescribed functions. In this review, we highlight how a number of protein functions are facilitated by intrinsic disorder and introduce a new protein structure taxonomy that is based on quantifiable metrics of a protein's disorder.
Keywords:
biophysics; conformational change; intrinsically disordered protein; protein folding; protein structure.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Amino Acids / chemistry*
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Amino Acids / metabolism
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CREB-Binding Protein / chemistry*
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CREB-Binding Protein / genetics
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CREB-Binding Protein / metabolism
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Colicins / chemistry*
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Colicins / genetics
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Colicins / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Eukaryotic Initiation Factors / chemistry*
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Eukaryotic Initiation Factors / genetics
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Eukaryotic Initiation Factors / metabolism
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Humans
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Intrinsically Disordered Proteins / chemistry*
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Intrinsically Disordered Proteins / genetics
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Intrinsically Disordered Proteins / metabolism
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Protein Binding
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Protein Folding
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Protein Interaction Domains and Motifs
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Protein Structure, Secondary
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Structure-Activity Relationship
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Thermodynamics
Substances
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Amino Acids
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Colicins
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EIF4EBP2 protein, human
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Eukaryotic Initiation Factors
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Intrinsically Disordered Proteins
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immE9 protein, E coli
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CREB-Binding Protein
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CREBBP protein, human
Associated data
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PDB/1bh4
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PDB/1jjs
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PDB/1k7b
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PDB/1kbh
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PDB/1qjp
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PDB/1ujw
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PDB/1zoq
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PDB/2c52
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PDB/2ivz
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PDB/2k3g
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PDB/2k3j
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PDB/2kac
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PDB/2kkj
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PDB/2l14
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PDB/2mx4
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PDB/3O0e
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PDB/3am7