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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.
Rakesh Trivedi, Hampapathalu Adimurthy Nagarajaram   +1 more
exaly   +4 more sources

Intrinsically disordered proteins and biomineralization [PDF]

Matrix Biology, 2016
In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele L Boskey, Eduardo Villarreal-Ramírez   +1 more
exaly   +3 more sources

Classification of Intrinsically Disordered Regions and Proteins

Chemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Robin Van Der Lee, Benjamin Lang, Gary W Daughdrill   +2 more
exaly   +4 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
openaire   +2 more sources

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

Molecular BioSystems, 2011
M. Madan Babu introduces this Molecular BioSystems themed issue on intrinsically disordered proteins.
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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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Translocation of polyampholytes and intrinsically disordered proteins⋆

The European Physical Journal E, 2018
Polyampholytes are polymers carrying electrical charges of both signs along their backbone. We consider synthetic polyampholytes with a quenched random charge sequence and intrinsically disordered proteins, which have a well-defined charge sequence and behave like polyampholytes in the denaturated state.
Johner, Albert, Joanny, Jean-François
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Intrinsically disordered proteins: regulation and disease

Current Opinion in Structural Biology, 2011
Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit interaction with several proteins and hence the re-use of the same protein in multiple pathways. Understanding IDP regulation is important because altered expression of IDPs is associated with many diseases. Recent studies show
Babu, M.M., Lee, R.T.J.G. van der, Groot, N.S. de, Gsponer, J.   +3 more
openaire   +2 more sources