Results 171 to 180 of about 1,763,945 (204)
Accurate interdomain contacts in a mixed folded protein from NMR-guided coarse-grained simulations.
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Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs) [PDF]
Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions.
Zanxia Cao
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Introduction to Intrinsically Disordered Proteins (IDPs)
Chemical Reviews, 2014Vladimir Uversky
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The Journal of Biochemistry, 2023
Abstract Relating the amino acid composition and sequence to chain folding and binding preferences of intrinsically disordered proteins (IDPs) has emerged as a huge challenge. While globular proteins have respective 3D structures that are unique to their individual functions, IDPs violate this structure–function paradigm because rather ...
Mujahid Hossain +2 more
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Abstract Relating the amino acid composition and sequence to chain folding and binding preferences of intrinsically disordered proteins (IDPs) has emerged as a huge challenge. While globular proteins have respective 3D structures that are unique to their individual functions, IDPs violate this structure–function paradigm because rather ...
Mujahid Hossain +2 more
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Intrinsically Disordered Proteins (IDP): Purification Under Denaturing Conditions
2022Recombinant protein expression in E. coli often induces the expressed protein to accumulate in insoluble aggregates, named inclusion bodies (IBs), that represent easy to isolate, highly pure protein reservoirs. IBs can be solubilized by denaturing agents but this procedure requires, for complex globular proteins, a refolding step that can be ...
Mireia, Pesarrodona +2 more
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Intrinsically disordered proteins (IDP) and metal ions: the case of amylin (HiAPP)
SMART eLAB, 2021poster presented at 1st Conference on Crystallography, Structural Chemistry and Biosystems, (Catania)
Macrì, Antonio +5 more
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Progress in Biophysics and Molecular Biology, 2015
In this review we discuss recent progress in targeting the protein-protein interactions made by oncogenic transcription factors. We particularly focus on the challenges posed by the prevalence of intrinsically disordered regions in this class of protein and the strategies being used to overcome them.
Giovanna Zinzalla
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In this review we discuss recent progress in targeting the protein-protein interactions made by oncogenic transcription factors. We particularly focus on the challenges posed by the prevalence of intrinsically disordered regions in this class of protein and the strategies being used to overcome them.
Giovanna Zinzalla
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[Intrinsically disordered proteins (IDPs) and the impact on cell stress resistance].
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2022Intrinsically disordered proteins (IDPs) are proteins or protein regions that fail to get folded into definite three-dimensional structures but participate in various biological processes and perform specific functions. Defying the traditional protein "sequence-structure-function" paradigm, they enrich the protein "structure-function" diversity ...
Ning, Yan +5 more
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Journal of Magnetic Resonance, 2015
Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%) of eukaryotic proteins has disordered regions of more than 50 amino acids in length.
Bernhard Brutscher +2 more
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Intrinsically disordered proteins (IDPs) are functional proteins containing large fragments characterized by high local mobility. Bioinformatic studies have suggested that a significant fraction (more than 30%) of eukaryotic proteins has disordered regions of more than 50 amino acids in length.
Bernhard Brutscher +2 more
exaly +4 more sources

