Results 21 to 30 of about 40,484 (286)
Protein flexibility and intrinsic disorder [PDF]
Protein Science, 2004 AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P. +7 more
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MobiDB: intrinsically disordered proteins in 2021 [PDF]
Nucleic Acids Research, 2020 AbstractThe MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process.
Damiano Piovesan +14 more
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Functionally Relevant Macromolecular Interactions of Disordered Proteins [PDF]
, 2020 Disordered proteins are relatively recent newcomers in protein science. They were first described in detail by Wright and Dyson, in their J. Mol. Biol. paper in 1999.
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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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Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]
, 2009 Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Edwards, Y.J.K. +11 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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Intrinsically disordered proteins: modes of binding with emphasis on disordered domains
Open Biology, 2021 Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris +2 more
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Self‐recognition by an intrinsically disordered protein [PDF]
FEBS Letters, 2008 The intrinsically disordered translocation domain (T‐domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T‐domain of colicin N known to bind to the helper protein TolA in target cells also ...
Hecht O +7 more
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Intrinsically Disordered Proteins in Chronic Diseases
Biomolecules, 2019 It is now increasingly evident that a large fraction of the human proteome comprises proteins that, under physiological conditions, lack fixed, ordered 3D structures as a whole or have segments that are not likely to form a defined 3D structure [...]
Prakash Kulkarni, Vladimir N. Uversky
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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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