Results 21 to 30 of about 3,841,423 (288)
Frontiers in Aging Neuroscience, 2022 Protein structure is determined by the amino acid sequence and a variety of post-translational modifications, and provides the basis for physiological properties.
Akshatha Ganne +7 more
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Structural characterization of intrinsically disordered proteins by NMR spectroscopy. [PDF]
, 2013 Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Contreras-Martos, Sara +7 more
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Biophysics and Physicobiology, 2020 Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically disordered regions.
Hiroto Anbo +2 more
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Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis. [PDF]
PLoS Computational Biology, 2009 We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes.
Jessica H Fong +5 more
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Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family [PDF]
, 2013 Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng +19 more
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Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]
PLoS ONE, 2013 The abundance and potential functional roles of intrinsically disordered regions in aquaporin-4, Kir4.1, a dystrophin isoforms Dp71, α-1 syntrophin, and α-dystrobrevin; i.e., proteins constituting the functional core of the astrocytic dystrophin ...
Insung Na +5 more
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Intrinsic disorder in putative protein sequences [PDF]
Proteome Science, 2011 Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradovic
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Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions
Molecules, 2017 Intrinsically disordered proteins and proteins with intrinsically disordered regions have been shown to be highly prevalent in disease. Furthermore, disease-causing expansions of the regions containing tandem amino acid repeats often push repetitive ...
April L. Darling, Vladimir N. Uversky
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Nature Communications, 2021 The intrinsically disordered acidic activation domain (AD) of the yeast transcription factor Gal4 acts through binding to the Med15 subunit of the Mediator complex.
Lisa M. Tuttle +5 more
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idpr: A package for profiling and analyzing Intrinsically Disordered Proteins in R
PLoS ONE, 2022 Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are proteins or protein-domains that do not have a single native structure, rather, they are a class of flexible peptides that can rapidly adopt multiple conformations ...
William M. McFadden, Judith L. Yanowitz
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