Multiple Structural States Exist Throughout the Helical Nucleation Sequence of the Intrinsically Disordered Protein Stathmin, As Reported by Electron Paramagnetic Resonance Spectroscopy. Kamel, Estefania Larrosa, Amissi Sadiki, and Michael D. Intrinsically Disordered Proteins as Important Players during Desiccation Stress of Soybean Radicles.
Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins. Journal of Chemical Theory and Computation 2019, 15 General Purpose Water Model Can Improve Atomistic Simulations of Intrinsically Disordered Proteins. Seifpanahi Shabane, Saeed Izadi, Alexey V. Journal of the American Society for Mass Spectrometry 2020, 31 Correlation between Labeling Yield and Surface Accessibility in Covalent Labeling Mass Spectrometry. Microsecond Simulation of the Proteoglycan-like Region of Carbonic Anhydrase IX and Design of Chemical Inhibitors Targeting pH Homeostasis in Cancer Cells.
Van Bibber, Cornelia Haerle, Roy Khalife, Guy W. Comprehensive Intrinsic Disorder Analysis of 6108 Viral Proteomes: From the Extent of Intrinsic Disorder Penetrance to Functional Annotation of Disordered Viral Proteins.
Naveen Kumar, Rahul Kaushik, Chandana Tennakoon, Vladimir N.Intrinsically Disordered Proteins: Critical Components of the Wetware. Prakash Kulkarni, Supriyo Bhattacharya, Srisairam Achuthan, Amita Behal, Mohit Kumar Jolly, Sourabh Kotnala, Atish Mohanty, Govindan Rangarajan, Ravi Salgia, Vladimir Uversky.This article is cited by 373 publications. The unexpectedly high frequency of mostly disordered proteins in eukaryotes has important implications both for large-scale, high-throughput projects and also for focused experiments aimed at determination of protein structure and function. Application of the consensus method to whole genomes reveals that approximately 4.5% of Yersinia pestis, 5% of Escherichia coli K12, 6% of Archaeoglobus fulgidus, 8% of Methanobacterium thermoautotrophicum, 23% of Arabidopsis thaliana, and 28% of Mus musculus proteins are mostly disordered. A new prediction method based on consensus is described. Each of these methods is reexamined, and the prediction results are compared herein. These methods are based on the net charge−hydropathy distribution and disorder prediction score distribution. Two distinct methods have been previously described for using amino acid sequences to predict which proteins are likely to be mostly disordered. Proteins with disordered regions are especially common in eukaryotic cells, with a subset of these proteins being mostly disordered, e.g., with more disordered than ordered residues. Intrinsically disordered proteins and regions carry out varied and vital cellular functions.
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