Cargando…
Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings
Although improved strategies for the detection and analysis of evolutionary couplings (ECs) between protein residues already enable the prediction of protein structures and interactions, they are mostly restricted to conserved and well-folded proteins. Whereas intrinsically disordered proteins (IDPs...
Autores principales: | Pancsa, Rita, Zsolyomi, Fruzsina, Tompa, Peter |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6274761/ https://www.ncbi.nlm.nih.gov/pubmed/30366362 http://dx.doi.org/10.3390/ijms19113315 |
Ejemplares similares
-
DisCons: a novel tool to quantify and classify evolutionary conservation of intrinsic protein disorder
por: Varadi, Mihaly, et al.
Publicado: (2015) -
Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins
por: Varadi, Mihaly, et al.
Publicado: (2015) -
Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability
por: Pancsa, Rita, et al.
Publicado: (2016) -
Synonymous Constraint Elements Show a Tendency to Encode Intrinsically Disordered Protein Segments
por: Macossay-Castillo, Mauricio, et al.
Publicado: (2014) -
Structural Disorder in Eukaryotes
por: Pancsa, Rita, et al.
Publicado: (2012)