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From molecular descriptions to cellular functions of intrinsically disordered protein regions. [PDF]

Biophys Rev (Melville)
Chen W, Fraser OA, George C, Showalter SA.   +3 more
europepmc   +1 more source

Intrinsically Disordered Proteins: An Overview

International Journal of Molecular Sciences, 2022
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions.
Hampapathalu Adimurthy Nagarajaram, Rakesh Trivedi   +1 more
exaly   +3 more sources

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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
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Intrinsically disordered protein

Journal of Molecular Graphics and Modelling, 2001
Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the random coil. The five following examples suggest that native protein structure can correspond to any of the three states (not just the ordered state) and that protein function can arise from any of the three states and their transitions.
A K, Dunker, J D, Lawson, C J, Brown, R M, Williams, P, Romero, J S, Oh, C J, Oldfield, A M, Campen, C M, Ratliff, K W, Hipps, J, Ausio, M S, Nissen, R, Reeves, C, Kang, C R, Kissinger, R W, Bailey, M D, Griswold, W, Chiu, E C, Garner, Z, Obradovic   +19 more
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Intrinsic disorder in S100 proteins

Molecular BioSystems, 2011
Abstract Although the members of the largest subfamily of the EF-hand proteins, S100 proteins, are evolutionarily young, their functional diversity is extremely broad, partly due to their ability to adapt to various targets. This feature is a hallmark of intrinsically disordered proteins (IDPs), but none of the S100 proteins are ...
Sergei E, Permyakov, Ramis G, Ismailov, Bin, Xue, Alexander I, Denesyuk, Vladimir N, Uversky, Eugene A, Permyakov   +5 more
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Intrinsically Disordered Proteins: An Update

2007 IEEE 7th International Symposium on BioInformatics and BioEngineering, 2007
Just over 10 years ago, in June, 1997, in the Proceedings of the IEEE International Conference on Neural Networks, we published our first predictor of intrinsically disordered protein. Since then, we have substantially improved our predictors, and more than 20 other laboratory groups have joined in efforts to improve the prediction of protein disorder.
A. Keith Dunker, Christopher J. Oldfield, Jingwei Meng, Pedro Romero, Jack Y. Yang, Zoran Obradovic, Vladimir N. Uversky   +6 more
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Intrinsically disordered proteins

Molecular BioSystems, 2011
M. Madan Babu introduces this Molecular BioSystems themed issue on intrinsically disordered proteins.
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Intrinsic Fluorescence of Intrinsically Disordered Proteins

2012
Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, CIURLI, STEFANO LUCIANO
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Exploring Protein Intrinsic Disorder with MobiDB

2020
Nowadays, it is well established that many proteins or regions under physiological conditions lack a fixed three-dimensional structure and are intrinsically disordered. MobiDB is the main repository of protein disorder and mobility annotations, combining different data sources to provide an exhaustive overview of intrinsic disorder.
Monzon A. M., Hatos A., Necci M., Piovesan D., Tosatto S. C. E.   +4 more
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