Results 111 to 120 of about 4,606,382 (149)
Long-lived States in an intrinsically disordered protein domain
Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is ...
Fernandes, L. +5 more
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A study of Protean Segments (ProSs):- Short regions in Intrinsically Disordered Proteins (IDPs) that undergo disorder-to-order transitions upon bindingopenaire +1 more source
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Chemical Reviews, 2014 It has long been axiomatic that a protein’s structure determines its function. Intrinsically disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure–function paradigm. They do not exhibit stable secondary and/or tertiary structures and exist as dynamic ensembles of interconverting conformers with preferred, nonrandom ...
Gary J Pielak +2 more
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Introduction to Intrinsically Disordered Proteins (IDPs)
Chemical Reviews, 2014Vladimir Uversky
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Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs) [PDF]
International Journal of Molecular Sciences, 2011 Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as tumor, Parkinson disease, Alzheimer disease, diabetes, and so on.
Liling Zhao, Zanxia Cao
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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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Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins
Biomolecules, 2018 Intrinsically disordered proteins (IDPs) are often modeled using ideas from polymer physics that suggest they smoothly explore all corners of configuration space.
Prakash Kulkarni +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
exaly +4 more sources