Results 161 to 170 of about 23,171 (195)
Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers. [PDF]
Byrd EJ +9 more
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Introduction to Intrinsically Disordered Proteins (IDPs)
Chemical Reviews, 2014Vladimir Uversky
exaly +5 more sources
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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ChemBioChem, 2012
AbstractCarbon‐13 direct‐detection NMR methods have proved to be very useful for the characterization of intrinsically disordered proteins (IDPs). Here we present a suite of experiments in which amino‐acid‐selective editing blocks are encoded in CACON‐ and CANCO‐type sequences to give 13C‐detected spectra containing correlations arising from a ...
Roberta Pierattelli +2 more
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AbstractCarbon‐13 direct‐detection NMR methods have proved to be very useful for the characterization of intrinsically disordered proteins (IDPs). Here we present a suite of experiments in which amino‐acid‐selective editing blocks are encoded in CACON‐ and CANCO‐type sequences to give 13C‐detected spectra containing correlations arising from a ...
Roberta Pierattelli +2 more
exaly +5 more sources
Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR
, 2018Intrinsically disordered proteins (IDPs) play important physiological, but also disease-related roles. In order to understand the function and malfunction of proteins of this class, electron paramagnetic resonance (EPR) spectroscopy has proven to be a valuable tool, allowing investigation of the protein structural ensembles upon interaction with the ...
Sabrina Weickert +2 more
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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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Rational drug design targeting intrinsically disordered proteins
WIREs Computational Molecular Science, 2023Intrinsically disordered proteins (IDPs) are proteins that perform important biological functions without well‐defined structures under physiological conditions.
Hanping Wang, Ruoyao Xiong, L. Lai
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