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Fine structures of Intrinsically Disordered Proteins [PDF]
The Journal of Chemical Physics, 2023 We report simulation studies of 33 single intrinsically disordered proteins (IDPs) using coarse-grained bead-spring models where interactions among different amino acids are introduced through a hydropathy matrix and additional screened Coulomb interaction for the charged amino acid beads. Our simulation studies of two different hydropathy scales (HPS1,
Swarnadeep Seth +2 more
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Intrinsically disordered proteins [PDF]
Mol. BioSyst., 2012 Our understanding of protein function has been predominated by the view that proteins need to adopt a defined three dimensional structure to be able to carry out their function. Indeed, crystal structures of numerous proteins have been instrumental in establishing the structure– function paradigm.
Agnieszka, Dziedzic-Letka +1 more
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Introducing Protein Intrinsic Disorder [PDF]
Chemical Reviews, 2014 No ...
Habchi, Johnny +3 more
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Intrinsically Disordered Proteins [PDF]
Cell, 2013 In the same way that neither a messy lab bench nor a clean one is a reliable indicator of a researcher’s productivity, a protein’s function cannot be judged solely on the basis of its neatly folded and stable domains. As evidenced by recent work discussed in this Select, we are learning that intrinsically disordered regions feature in many of the cell ...
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Databases for intrinsically disordered proteins [PDF]
Acta Crystallographica Section D Structural Biology, 2022 Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano +3 more
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Open questions: Reflections on intrinsically disordered proteins [PDF]
Network Biology, 2021 Intrinsically Disordered Proteins or Regions (IDPs) are proteins that lack a predetermined 3D structure playing key cellular functions including regulation, signaling, and protein-protein/DNA interaction.
Mouna Choura, Ahmed Rebai
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
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Ensemble Docking for Intrinsically Disordered Proteins. [PDF]
J Chem Inf ModelAbstractIntrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable for IDPs.
Dhar A, Sisk TR, Robustelli P.
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Frontiers in Molecular Biosciences, 2015 Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles.
Gabriel eThieulin-Pardo +3 more
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Intrinsically disordered proteins: modes of binding with emphasis on disordered domains
Open Biology, 2021 Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris +2 more
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