Results 31 to 40 of about 32,287 (136)
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
Intrinsically Disordered Proteins and the Janus Challenge
Biomolecules, 2018 To gain a new insight into the role of proteins in the origin of life on Earth, we present the Janus Challenge: identify an intrinsically disordered protein (IDP), naturally occurring or synthetic, that has catalytic activity.
Prakash Kulkarni, Vladimir N. Uversky
doaj +1 more source
Function, Regulation, and Dysfunction of Intrinsically Disordered Proteins
Life, 2021 The discovery that a considerable fraction of the eukaryotic proteins lacks a well-defined three-dimensional structure in their native state has revolutionised our general understanding of proteins [...]
Giuliana Fusco, Stefano Gianni
doaj +1 more source
Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. [PDF]
PLoS ONE, 2011 BACKGROUND: Intrinsically disordered regions are enriched in short interaction motifs that play a critical role in many protein-protein interactions. Since new short interaction motifs may easily evolve, they have the potential to rapidly change protein ...
Floriane Montanari +2 more
doaj +1 more source
Protein flexibility and intrinsic disorder [PDF]
Protein Science, 2004 AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P. +7 more
openaire +4 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 +1 more source
Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology
Biomolecules, 2023 Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late 1990s when a few groups, working independently, convinced the community that these ‘weird’ proteins could have important functions.
Rachel Evans +3 more
doaj +1 more source
Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]
PLoS ONE, 2013 The abundance and potential functional roles of intrinsically disordered regions in aquaporin-4, Kir4.1, a dystrophin isoforms Dp71, α-1 syntrophin, and α-dystrobrevin; i.e., proteins constituting the functional core of the astrocytic dystrophin ...
Insung Na +5 more
doaj +1 more source
Intrinsically Disordered Proteins: An Overview
International Journal of Molecular Sciences, 2022 Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions.
Rakesh Trivedi +1 more
openaire +2 more sources
Intrinsically disordered proteins and biomineralization [PDF]
Matrix Biology, 2016 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 +1 more
openaire +2 more sources