Results 51 to 60 of about 448,472 (368)

Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. [PDF]

open access: yesPLoS 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

Function, Regulation, and Dysfunction of Intrinsically Disordered Proteins

open access: yesLife, 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

Salt-dependent conformational changes of intrinsically disordered proteins

open access: yesbioRxiv, 2021
The flexible structure of an intrinsically disordered protein (IDP) is known to be perturbed by salt concentrations, which can be understood by electrostatic screening on charged amino acids. However, an IDP usually contains more uncharged residues which
Samuel Wohl, M. Jakubowski, Wenwei Zheng
semanticscholar   +1 more source

Intrinsically Disordered Proteins at the Nano-scale [PDF]

open access: yesNano Futures 5(2), 022501 (2021), 2021
The human proteome is enriched in proteins that do not fold into a stable 3D structure. These intrinsically disordered proteins (IDPs) spontaneously fluctuate between a large number of configurations in their native form. Remarkably, the disorder does not lead to dysfunction as with denatured folded proteins.
arxiv   +1 more source

Comparative roles of charge, π, and hydrophobic interactions in sequence-dependent phase separation of intrinsically disordered proteins [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2020
Significance Mesoscopic condensates of proteins and nucleic acids, including membraneless organelles, serve myriad biological functions, whereas dysregulation of condensates can cause disease.
Suman Das   +4 more
semanticscholar   +1 more source

Conformational Recognition of an Intrinsically Disordered Protein [PDF]

open access: yesBiophysical Journal, 2014
There is a growing interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the characterization of these states remains an open challenge. IDPs appear to have functional roles that diverge from those of folded proteins and revolve around their ability to act as hubs for protein-protein interactions.
Stephan M. Feller   +9 more
openaire   +4 more sources

Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]

open access: yesPLoS 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

Recruitment of mRNAs to P granules by condensation with intrinsically-disordered proteins

open access: yeseLife, 2020
RNA granules are protein/RNA condensates. How specific mRNAs are recruited to cytoplasmic RNA granules is not known. Here, we characterize the transcriptome and assembly of P granules, RNA granules in the C. elegans germ plasm.
C. Lee   +5 more
semanticscholar   +1 more source

What’s in a name? Why these proteins are intrinsically disordered [PDF]

open access: yesIntrinsically Disordered Proteins, 2013
"What's in a name? That which we call a rose By any other name would smell as sweet." From "Romeo and Juliet", William Shakespeare (1594) This article opens a series of publications on disambiguation of the basic terms used in the field of intrinsically disordered proteins. We start from the beginning, namely from the explanation of what the expression
Sonia Longhi   +24 more
openaire   +3 more sources

Critical Assessment of Protein Intrinsic Disorder Prediction [PDF]

open access: yesNature Methods, 2020
AbstractIntrinsically disordered proteins defying the traditional protein structure-function paradigm represent a challenge to study experimentally. As a large part of our knowledge rests on computational predictions, it is crucial for their accuracy to be high.
Necci, Marco   +99 more
openaire   +13 more sources

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