Results 251 to 260 of about 1,883,575 (282)

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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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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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
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Druggability of Intrinsically Disordered Proteins

2015
Although the proteins in all the current major classes considered to be druggable are folded in their native states, intrinsically disordered proteins (IDPs) are becoming attractive candidates for therapeutic intervention by small drug-like molecules.
Priyanka, Joshi, Michele, Vendruscolo
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Intrinsically disordered proteins

This chapter explores intrinsically disordered proteins (IDPs), detailing their discovery, structural characteristics, and indispensable biological functions. It introduces the hypothesis that unfolded proteins can bind diverse partners, first proposed in 1939, and follows the experimental validation of IDPs using NMR and X-ray methods.
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Intrinsic Disorder and Protein Function

Biochemistry, 2002
A Keith, Dunker, Celeste J, Brown, J David, Lawson, Lilia M, Iakoucheva, Zoran, Obradović   +4 more
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