Results 1 to 10 of about 754 (67)
Biophysics and Physicobiology, 2020 Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions.
Hiroto Anbo +2 more
doaj +2 more sources
PLoS ONE, 2019 Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana +3 more
doaj +2 more sources
The Origin of Discrepancies between Predictions and Annotations in Intrinsically Disordered Proteins
Biomolecules, 2023 Disorder prediction methods that can discriminate between ordered and disordered regions have contributed fundamentally to our understanding of the properties and prevalence of intrinsically disordered proteins (IDPs) in proteomes as well as their ...
Mátyás Pajkos +2 more
doaj +1 more source
Prediction of folding patterns for intrinsic disordered protein
Scientific Reports, 2023 The conformation flexibility of natural protein causes both complexity and difficulty to understand the relationship between structure and function. The prediction of intrinsically disordered protein primarily is focusing on to disclose the regions with ...
Jiaan Yang +4 more
doaj +1 more source
Epichromatin and chromomeres: a ‘fuzzy’ perspective [PDF]
Open Biology, 2018 ‘Epichromatin’, the surface of chromatin beneath the interphase nuclear envelope (NE) or at the surface of mitotic chromosomes, was discovered by immunostaining with a specific bivalent mouse monoclonal anti-nucleosome antibody (mAb PL2-6). ‘Chromomeres’,
Donald E. Olins, Ada L. Olins
doaj +1 more source
New insights into disordered proteins and regions according to the FOD-M model.
PLoS ONE, 2022 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
Evolutionary Study of Disorder in Protein Sequences
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely ...
Kristina Kastano +6 more
doaj +1 more source
Intrinsically disordered regions in TRPV2 mediate protein-protein interactions
Communications Biology, 2023 Transient receptor potential (TRP) ion channels are gated by diverse intra- and extracellular stimuli leading to cation inflow (Na+, Ca2+) regulating many cellular processes and initiating organismic somatosensation.
Raghavendar R. Sanganna Gari +6 more
doaj +1 more source
Biomolecules, 2022 The unique functions of intrinsically disordered proteins (IDPs) depend on their dynamic protean structure that often eludes analysis. High-speed atomic force microscopy (HS-AFM) can conduct this difficult analysis by directly visualizing individual IDP ...
Toshio Ando
doaj +1 more source
Proteome-wide signatures of function in highly diverged intrinsically disordered regions
eLife, 2019 Intrinsically disordered regions make up a large part of the proteome, but the sequence-to-function relationship in these regions is poorly understood, in part because the primary amino acid sequences of these regions are poorly conserved in alignments ...
Taraneh Zarin +5 more
doaj +1 more source