Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum
| Autor: | Diego O. Nolasco, Collin M. Stultz, Virginia M. Burger |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein Folding media_common.quotation_subject Colicins Plasma protein binding Computational biology Biology Intrinsically disordered proteins Biochemistry Protein Structure Secondary Structure-Activity Relationship 03 medical and health sciences Protein structure Escherichia coli Humans Protein Interaction Domains and Motifs Amino Acid Sequence Amino Acids Eukaryotic Initiation Factors Function (engineering) Molecular Biology Peptide sequence media_common Minireviews Cell Biology CREB-Binding Protein Protein tertiary structure Intrinsically Disordered Proteins Range (mathematics) 030104 developmental biology Thermodynamics Protein folding Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 291:6706-6713 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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