Results 51 to 60 of about 32,287 (136)
INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]
Biocomputing 2012, 2011 Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun, Hsu +7 more
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Mapping Charge Interactions in Intrinsically Disordered Proteins
Advanced ScienceIntrinsically disordered proteins (IDPs) are often rich in charged residues, and electrostatic interactions have a pronounced effect on their conformational distributions, interactions and functions.
Michael Phillips +14 more
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Intrinsically disordered proteins: controlled chaos or random walk
International Journal of Plant Biology, 2016 Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton +3 more
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F1000Research, 2020 Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in ...
Vladimir N. Uversky
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Protein intrinsic disorder in plants
Frontiers in Plant Science, 2013 To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions.
Pazos, Florencio +3 more
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Complex microparticle architectures from stimuli-responsive intrinsically disordered proteins
Nature Communications, 2020 The production of microparticles with complex geometries for biotechnological use historically requires sophisticated fabrication techniques. Here, the authors create complex particle geometries by exploiting the metastable region of the phase diagram of
Stefan Roberts +7 more
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Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins
Frontiers in Plant Science, 2012 Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signalling proteins such as receptor-like kinases (RLKs) and may ...
Macarena eMarín, Thomas eOtt
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Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis. [PDF]
PLoS Computational Biology, 2009 We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes.
Jessica H Fong +5 more
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Intrinsically Disordered Proteins: Gatekeepers of the Nuclear Pore Complex [PDF]
Biophysical Journal, 2016 The transport of molecules between the nucleus and the cytoplasm is facilitated by highly-selective nuclear pore complexes (NPCs) embedded in the nuclear envelope. The NPCs provide bidirectional pathways for passive and active (facilitated) transport. Active transport is facilitated by the binding of cargo to chaperons (i.e., transport factors or ‘kaps’
Ghavami, Ali +3 more
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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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