Results 41 to 50 of about 41,661 (301)
INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]
Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun Hsu +7 more
openaire +2 more sources
Inferring function using patterns of native disorder in proteins [PDF]
Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB +14 more
core +1 more source
Folding factors and partners for the intrinsically disordered protein Micro-Exon Gene 14 (MEG-14)
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera.
Orcia, Debora +17 more
core +1 more source
Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Contreras-Martos, Sara +7 more
core +1 more source
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng +19 more
core +1 more source
The function of intrinsically disordered selenoproteins
Rozovsky, SharonSELENOS and SELENOK are intrinsically disordered selenoproteins that take part in the endoplasmic-reticulum-associated degradation (ERAD) pathway, which degrades misfolded proteins and maintains cellular protein hemostasis.
Cheng, Rujin
core +1 more source
Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins [PDF]
Intrinsically disordered proteins (IDPs) are predicted to represent about one third of the eukaryotic proteome. The dynamic ensemble of conformations of this steadily growing class of proteins has remained hardly accessible for bulk biophysical ...
Rubén Hervás +8 more
core +1 more source
New insights into disordered proteins and regions according to the FOD-M model.
A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit ...
Irena Roterman +3 more
doaj +2 more sources
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878) +12 more
core +1 more source
Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G. +20 more
core +1 more source

