Results 61 to 70 of about 1,763,945 (204)
Frontiers in Molecular Biosciences, 2014 Biologically active proteins without stable tertiary structure are common in all known proteomes. Functions of these intrinsically disordered proteins (IDPs) are typically related to regulation, signaling and control.
Vladimir N. Uversky
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Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities. [PDF]
PLoS Computational Biology, 2016 The properties of disordered proteins are thought to depend on intrinsic conformational propensities for polyproline II (PPII) structure. While intrinsic PPII propensities have been measured for the common biological amino acids in short peptides, the ...
Maria E Tomasso +3 more
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FEBS Open Bio, EarlyView.We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
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Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy
Biomolecules, 2020 Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as ...
Do-Hyoung Kim +4 more
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npj Systems Biology and Applications, 2023 Intrinsically disordered proteins (IDPs), which can interact with many partner proteins, are central to many physiological functions and to various pathologies that include neurodegeneration. Here, we introduce the Sherpa hypothesis, according to which a
Vic Norris +4 more
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Advanced Materials, EarlyView.Cancer‐associated NPC remodeling creates a high‐flux, low‐stringency nuclear state that supports malignant adaptation but increases mechanical fragility. Targeting the FG‐barrier or NPC scaffold may drive mechanostat failure, envelope rupture, DNA damage, and loss of nuclear integrity.
Sílvio Terra Stefanello +5 more
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A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43
Advanced Science, EarlyView.Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg +16 more
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BMC BiologyIntrinsically disordered proteins (IDPs) and biomolecular condensates are critical for cellular processes and physiological functions. Abnormal biomolecular condensates can cause diseases such as cancer and neurodegenerative disorders.
Caolitao Qin +4 more
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Intrinsically Disordered Side of the Zika Virus Proteome
Frontiers in Cellular and Infection Microbiology, 2016 Over the last few decades, concepts of protein intrinsic disorder have been implicated in different biological processes. Recent studies have suggested that intrinsically disordered proteins (IDPs) provide structural plasticity and functional diversity ...
Rajanish Giri +3 more
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A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers
Advanced Science, EarlyView.Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Jasper J. Michels +2 more
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