Results 41 to 50 of about 1,763,945 (204)
Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
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A novel mode of interaction between intrinsically disordered proteins
Biophysics and Physicobiology, 2020 An increasing number of proteins, which have neither regular secondary nor well-defined tertiary structures, have been found to be present in cells. The structure of these proteins is highly flexible and disordered under physiological (native) conditions,
Emi Hibino, Masaru Hoshino
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Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]
, 2009 Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Edwards, Y.J.K. +11 more
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The IDP-Specific Force Field ff14IDPSFF Improves the Conformer Sampling of Intrinsically Disordered Proteins [PDF]
Journal of Chemical Information and Modeling, 2017 Intrinsically disordered proteins (IDPs) or intrinsically disordered regions do not have a fixed tertiary structure but play key roles in signal regulation, molecule recognition, and drug targeting. However, it is difficult to study the structure and function of IDPs by traditional experimental methods because of their diverse conformations ...
Dong Song, Ray Luo 0001, Hai-Feng Chen
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Frontiers in Genetics, 2018 Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are functional proteins and domains that devoid stable secondary and/or tertiary structure.
April L. Darling +2 more
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The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid. [PDF]
, 2013 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
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Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Frontiers in Physics, 2019 Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
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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
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PLoS ONE, 2023 Intrinsically disordered proteins (IDPs) are proteins that lack a stable 3D structure but maintain a biological function. It has been frequently suggested that IDPs are difficult to align because they tend to have fewer conserved residues compared to ...
Andrew C Riley +2 more
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Inferring function using patterns of native disorder in proteins [PDF]
, 2007 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
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