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Titlebook: Intrinsically Disordered Proteins Studied by NMR Spectroscopy; Isabella C. Felli,Roberta Pierattelli Book 2015 The Editor(s) (if applicabl

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Recombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks,availability to allow the characterization of their structural and dynamic properties. The sample preparation is therefore the limiting step to allow any biophysical method being able to characterize the properties of an intrinsically disordered protein and to clarify the links between these propert
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Bioinformatics Approaches for Predicting Disordered Protein Motifs,ot more than 10 consecutive amino acids in length with less than 5 defined positions. Many positions are ‘degenerate’ thus offering flexibility in terms of the amino acid types allowed at those positions. Their short length and degenerate nature confers evolutionary plasticity meaning that SLiMs oft
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The Protein Ensemble Database,gm due to the emergence of intrinsically disordered proteins (IDPs). As opposed to their folded cousins, these proteins are defined by the lack of a stable 3D fold and a high degree of inherent structural heterogeneity that is closely tied to their function. Due to their flexible nature, solution te
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Order and Disorder in the Replicative Complex of Paramyxoviruses, paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. We provide a detailed description of the molecular mechanisms that govern the disorder-to-order transition that the intrinsically disordered C-terminal domain (N.) of their N proteins undergoes upon binding to the C-te
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,Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer’s Disease,nd Alzheimer’s disease (AD) in particular. Although the direct involvement of Aβ peptides in AD is well documented and their aggregative ability is closely related to their neurotoxicity, the precise mechanism of the neurotoxic effects of Aβ peptides remains unclear. There is still a significant gap
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