Results 331 to 340 of about 448,472 (368)

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.
C. Oldfield, A. Dunker
semanticscholar   +4 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
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 recognized as IDPs.
Alexander I. Denesyuk, Alexander I. Denesyuk, Bin Xue, Bin Xue, Sergei E. Permyakov, Eugene A. Permyakov, Ramis G. Ismailov, Vladimir N. Uversky   +7 more
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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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Recent Developments in the Field of Intrinsically Disordered Proteins: Intrinsic Disorder-Based Emergence in Cellular Biology in Light of the Physiological and Pathological Liquid-Liquid Phase Transitions.

Annual Review of Biophysics, 2021
This review deals with two important concepts-protein intrinsic disorder and proteinaceous membrane-less organelles (PMLOs). The past 20 years have seen an upsurge of scientific interest in these phenomena.
V. Uversky
semanticscholar   +1 more source

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: 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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Single-Molecule FRET of Intrinsically Disordered Proteins.

Annual review of physical chemistry (Print), 2020
Intrinsically disordered proteins (IDPs) are now widely recognized as playing critical roles in a broad range of cellular functions as well as being implicated in diverse diseases.
L. Metskas, E. Rhoades
semanticscholar   +1 more source

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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Comparison and Evaluation of Force Fields for Intrinsically Disordered Proteins

Journal of Chemical Information and Modeling, 2020
Molecular dynamics (MD) simulations of six upgraded empirical force fields were compared and evaluated with short peptides, intrinsically disordered proteins and folded proteins using trajectories of 1, 1.5, 5 or 10μs (5 replicates of 200ns, 300ns, 1μs ...
M. Rahman, A. Rehman, Hao Liu, Haifeng Chen   +3 more
semanticscholar   +1 more source