Sequence-Dependent Conformational Landscapes of Intrinsically Disordered Proteins Reveal Asymmetric Chain Compaction. [PDF]
Wang C, Zhang B.
europepmc +1 more source
Membrane Association of Intrinsically Disordered Proteins. [PDF]
MacAinsh M +3 more
europepmc +1 more source
Correlated Segments of Intrinsically Disordered Proteins as Drivers of Homotypic Phase Separation. [PDF]
Zhou HX.
europepmc +1 more source
DIRseq as a method for predicting drug-interacting residues of intrinsically disordered proteins from sequences. [PDF]
MacAinsh M, Qin S, Zhou HX.
europepmc +1 more source
Correction to: Intrinsic stiffness and <i>Θ</i>-solvent regime in intrinsically disordered proteins: Implications for liquid-liquid phase separation. [PDF]
europepmc +1 more source
Intrinsically Disordered Proteins: An Overview
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states.
Hampapathalu A Nagarajaram +1 more
exaly +4 more sources
Intrinsically Disordered Proteins and Proteins With Intrinsically Disordered Regions in Neurodegenerative Diseases [PDF]
Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled ...
Orkide Coşkuner-Weber, Vladimir Uversky
exaly +6 more sources
Intrinsically Disordered Proteins and Biomineralization [PDF]
In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele L. Boskey, Eduardo Villarreal
exaly +3 more sources
Classification of Intrinsically Disordered Regions and Proteins
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Benjamin Lang +2 more
exaly +4 more sources
Related searches:
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Annual Review of Biochemistry, 2014Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
openaire +2 more sources

