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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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On the Origins of Intrinsically Disordered Proteins [PDF]
Biophysical Journal, 2010 A large number of proteins are sufficiently unstable that their full three dimensional structure cannot be resolved. The origins of this intrinsic disorder are not well understood, but its ubiquitous presence undercuts the principle that a protein's structure determines its function.
Faeder R. James +2 more
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BMC Bioinformatics, 2017 Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu +8 more
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Evolutionary Study of Disorder in Protein Sequences
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely ...
Kristina Kastano +6 more
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How multisite phosphorylation impacts the conformations of intrinsically disordered proteins
PLoS Comput. Biol., 2021 Phosphorylation of intrinsically disordered proteins (IDPs) can produce changes in structural and dynamical properties and thereby mediate critical biological functions.
Fan Jin, F. Gräter
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Intrinsically disordered proteins and biomineralization [PDF]
Matrix Biology, 2016 In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Eduardo Villarreal-Ramírez +1 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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Frontiers in Aging Neuroscience, 2022 Protein structure is determined by the amino acid sequence and a variety of post-translational modifications, and provides the basis for physiological properties.
Akshatha Ganne +7 more
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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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Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
Life, 2020 In recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and ...
Frederik Lermyte
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