Results 41 to 50 of about 410,023 (357)
Physics-based computational and theoretical approaches to intrinsically disordered proteins.
Current Opinion in Structural Biology, 2021 Intrinsically disordered proteins (IDPs) are an important class of proteins that do not fold to a well-defined three-dimensional shape but rather adopt an ensemble of inter-converting conformations.
J. Shea, R. Best, J. Mittal
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A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome [PDF]
, 2013 This article is made available for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source.
Dunker, A. Keith +6 more
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
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Recent Force Field Strategies for Intrinsically Disordered Proteins
Journal of Chemical Information and Modeling, 2021 Intrinsically disordered proteins (IDPs) are widely distributed across eukaryotic cells, playing important roles in molecular recognition, molecular assembly, post-translational modification, and other biological processes.
Junxi Mu +4 more
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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 +3 more
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Targeting Intrinsically Disordered Proteins through Dynamic Interactions
Biomolecules, 2020 Intrinsically disordered proteins (IDPs) are over-represented in major disease pathways and have attracted significant interest in understanding if and how they may be targeted using small molecules for therapeutic purposes.
Jianlin Chen, Xiaorong Liu, Jianhan Chen
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Uncovering non-random binary patterns within sequences of intrinsically disordered proteins.
Journal of Molecular Biology, 2021 Sequence-ensemble relationships of intrinsically disordered proteins (IDPs) are governed by binary patterns such as the linear clustering or mixing of specific residues or residue types with respect to one another.
Megan C. Cohan +3 more
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BMC Bioinformatics, 2017 Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu +8 more
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On the roles of intrinsically disordered proteins and regions in cell communication and signaling
Cell Communication and Signaling, 2021 For proteins, the sequence → structure → function paradigm applies primarily to enzymes, transmembrane proteins, and signaling domains. This paradigm is not universal, but rather, in addition to structured proteins, intrinsically disordered proteins and ...
Sarah E. Bondos, A. Dunker, V. Uversky
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Constructing ensembles for intrinsically disordered proteins [PDF]
, 2011 The relatively flat energy landscapes associated with intrinsically disordered proteins makes modeling these systems especially problematic. A comprehensive model for these proteins requires one to build an ensemble consisting of a finite collection of ...
Fisher, Charles K., Stultz, Collin M.
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