Results 1 to 10 of about 1,240 (66)

Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell.

PLoS ONE, 2019
Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana, Sergio Forcelloni, Alessandro Porrello, Andrea Giansanti   +3 more
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Synergy between intrinsically disordered domains and structured proteins amplifies membrane curvature sensing

Nature Communications, 2018
Many proteins which sense membrane curvature contain intrinsically disordered domains. Here the authors use Monte Carlo simulations combined with experimental approaches and report that disordered domains are potent sensors of membrane curvature.
Wade F. Zeno, Upayan Baul, Wilton T. Snead, Andre C. M. DeGroot, Liping Wang, Eileen M. Lafer, D. Thirumalai, Jeanne C. Stachowiak   +7 more
doaj   +2 more sources

IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures

BMC Molecular and Cell Biology, 2022
Background Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions but play crucial roles in many biological processes.
CanZhuang Sun, YongE Feng, GuoLiang Fan
doaj   +1 more source

Investigating Intrinsically Disordered Proteins With Brownian Dynamics

Frontiers in Molecular Biosciences, 2022
Intrinsically disordered proteins (IDPs) have recently become systems of great interest due to their involvement in modulating many biological processes and their aggregation being implicated in many diseases.
Surl-Hee Ahn, Gary A. Huber, Gary A. Huber, J. Andrew McCammon, J. Andrew McCammon   +4 more
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idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R

PLoS ONE, 2022
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
doaj   +3 more sources

Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins

Biomolecules, 2020
Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali, Isabella C. Felli, Roberta Pierattelli   +2 more
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Evolutionary Study of Disorder in Protein Sequences

Biomolecules, 2020
Intrinsically disordered proteins (IDPs) contain regions lacking intrinsic globular structure (intrinsically disordered regions, IDRs). IDPs are present across the tree of life, with great variability of IDR type and frequency even between closely ...
Kristina Kastano, Gábor Erdős, Pablo Mier, Gregorio Alanis-Lobato, Vasilis J. Promponas, Zsuzsanna Dosztányi, Miguel A. Andrade-Navarro   +6 more
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NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences

Biophysics and Physicobiology, 2020
Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically dis­ordered regions.
Hiroto Anbo, Hiroki Amagai, Satoshi Fukuchi   +2 more
doaj   +1 more source

Fairy tails: Flexibility and function of intrinsically disordered extensions in the photosynthetic world

Frontiers in Molecular Biosciences, 2015
Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles.
Gabriel eThieulin-Pardo, Luisana eAvilan, Mila eKojadinovic, Brigitte eGontero   +3 more
doaj   +1 more source

Open questions: Reflections on intrinsically disordered proteins [PDF]

Network Biology, 2021
Intrinsically Disordered Proteins or Regions (IDPs) are proteins that lack a predetermined 3D structure playing key cellular functions including regulation, signaling, and protein-protein/DNA interaction.
Mouna Choura, Ahmed Rebai
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