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]

open access: yesAnal Chem
Byrd EJ   +9 more
europepmc   +1 more source

A study of Protean Segments (ProSs):- Short regions in Intrinsically Disordered Proteins (IDPs) that undergo disorder-to-order transitions upon binding

open access: yesA study of Protean Segments (ProSs):- Short regions in Intrinsically Disordered Proteins (IDPs) that undergo disorder-to-order transitions upon binding
openaire   +1 more source

Targeting Protein–Protein Interactions (PPIs) of Transcription Factors: Challenges of Intrinsically Disordered Proteins (IDPs) and Regions (IDRs)

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
exaly   +5 more sources

Exclusively Heteronuclear 13C-Detected Amino-Acid-Selective NMR Experiments for the Study of Intrinsically Disordered Proteins (IDPs)

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
exaly   +5 more sources

Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR

, 2018
Intrinsically 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
semanticscholar   +2 more sources

A three-state mechanism for trifluoroethanol denaturation of an intrinsically disordered protein (IDP)

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
openaire   +2 more sources

Intrinsically Disordered Proteins (IDP): Purification Under Denaturing Conditions

2022
Recombinant 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
openaire   +2 more sources

Intrinsically disordered proteins (IDP) and metal ions: the case of amylin (HiAPP)

SMART eLAB, 2021
poster presented at 1st Conference on Crystallography, Structural Chemistry and Biosystems, (Catania)
Macrì, Antonio   +5 more
openaire   +1 more source

Rational drug design targeting intrinsically disordered proteins

WIREs Computational Molecular Science, 2023
Intrinsically disordered proteins (IDPs) are proteins that perform important biological functions without well‐defined structures under physiological conditions.
Hanping Wang, Ruoyao Xiong, L. Lai
semanticscholar   +1 more source

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