Results 171 to 180 of about 1,763,945 (204)

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

Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs) [PDF]

open access: yesInternational 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.
Zanxia Cao
exaly   +7 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

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   +4 more sources

[Intrinsically disordered proteins (IDPs) and the impact on cell stress resistance].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2022
Intrinsically 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
openaire   +1 more source

Longitudinal relaxation properties of 1HN and 1Hα determined by direct-detected 13C NMR experiments to study intrinsically disordered proteins (IDPs)

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
exaly   +4 more sources

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