Results 201 to 210 of about 23,829 (240)

The cellular economy while crafting regulatory processes relies on protein intrinsic disorder: how and why precision comes at a cost in protein structure. [PDF]

Cell Commun Signal
Gupta MN, Uversky VN.
europepmc   +1 more source

The Monomeric Conformational Ensembles of Aβ40 and Aβ42 Encode Their Differential Amyloid Aggregation Propensity. [PDF]

J Phys Chem B
Cadenelli I, Ciccolo A, Tagliabue A, Rossi G, Conti Nibali V, Bochicchio D.   +5 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

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

Chemical Reviews, 2014
Vladimir N Uversky
exaly   +5 more sources

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 ...
Wolfgang Bermel, Jordan H Chill, Isabella C Felli   +2 more
exaly   +5 more sources

Diffusing protein binders to intrinsically disordered proteins

Nature
Proteins that bind to intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) with high affinity and specificity could be useful for therapeutic and diagnostic applications1, 2, 3–4.
Caixuan Liu, Kejia Wu, Hojun Choi, Hannah L. Han, Xueli Zhang, Joseph L. Watson, Green Ahn, Jason Z. Zhang, S. Shijo, Lydia L. Good, Charlotte M Fischer, A. Bera, A. Kang, Evans Brackenbrough, B. Coventry, Derrick R Hick, S. Qamar, Xinting Li, Justin Decarreau, Stacey R. Gerben, Wei Yang, Inna Goreshnik, Dionne K. Vafeados, Xinru Wang, M. Lamb, Analisa Murray, Sebastian Kenny, Magnus S. Bauer, Andy Hoofnagle, Ping Zhu, T. Knowles, David Baker   +31 more
semanticscholar   +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, Hongxing Li, Longhao Wu, Shuo Yang, Lujiang Hao, X. Bao   +5 more
semanticscholar   +3 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, J. Cattani, M. Drescher   +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, Noorul Huda, Abani K Bhuyan   +2 more
openaire   +2 more sources