Understanding the functional role of the intrinsically
... Higher eukaryotic proteomes contain extensive unstructured intrinsically disordered regions. These regions often control the localisation, stability and modification state of a protein. Yet, the functional role of ...
... Higher eukaryotic proteomes contain extensive unstructured intrinsically disordered regions. These regions often control the localisation, stability and modification state of a protein. Yet, the functional role of ...
Improving Function Prediction Using Patterns of Native Disorder in
... Instrinsically unstructured (disordered) proteins adopt little or no stable secondary structure in their native state. Proteins containing long disordered regions are abundant within eukaryotic genomes and can be predicted successfully from amino sequence. Disordered regions have been shown to be im ...
... Instrinsically unstructured (disordered) proteins adopt little or no stable secondary structure in their native state. Proteins containing long disordered regions are abundant within eukaryotic genomes and can be predicted successfully from amino sequence. Disordered regions have been shown to be im ...
Intrinsically disordered proteins
An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the last decades by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules.