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• W2057567541 endingPage "6714" @default.
• W2057567541 startingPage "6661" @default.
• W2057567541 abstract "It has long been axiomatic that a protein’s structure determines its function. Intrinsically disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure–function paradigm. They do not exhibit stable secondary and/or tertiary structures and exist as dynamic ensembles of interconverting conformers with preferred, nonrandom orientations.1-4 The concept of IDPs and IDRs as functional biological units was initially met with skepticism. For a long time, disorder, intuitively implying chaos, had no place in our perception of orchestrated molecular events controlling cell biology.Over the past years, however, this notion has changed. Aided by findings that structural disorder constitutes an ubiquitous and abundant biological phenomenon in organisms of all phyla,5-7 and that it is often synonymous with function,8-11 disorder has become an integral part of modern protein biochemistry. Disorder thrives in eukaryotic signaling pathways12 and functions as a prominent player in many regulatory processes.13-15 Disordered proteins and protein regions determine the underlying causes of many neurodegenerative disorders and constitute the main components of amyloid fibrils.16 They further contribute to many forms of cancer, diabetes and to cardiovascular and metabolic diseases.17,18Research into disordered proteins produced significant findings and established important new concepts. On the structural side, novel experimental and computational approaches identified and described disordered protein ensembles3,19,20 and led to terms such as secondary structure propensities, residual structural features, and transient long-range contacts.1,21 The discovery of coupled folding-and-binding reactions defined the paradigm of disorder-to-order transitions22 and high-resolution insights into the architectures of amyloid fibrils were obtained.23,24 On the biological side, we learned about the unexpected intracellular stability of disordered proteins, their roles in integrating post-translational protein modifications in cell signaling and about their functions in regulatory processes ranging from transcription to cell fate decisions.15,25,26 One open question remaining to be addressed is how these in vitro structural insights relate to biological in vivo effects. How do complex intracellular environments modulate the in vivo properties of disordered proteins and what are the implications for their biological functions (Figure 1)?27-29Figure 1Intracellular complexity. (A) Left: Cryo-electron tomography slice of a mammalian cell. Middle: Close-up view of cellular structures colored according to their identities: Right: Three-dimensional surface representation of the same region. Yellow, endoplasmic ...Here, we attempt to answer these questions by reviewing the physical and biological properties of intracellular environments in relation to structural and functional parameters of disordered proteins. Specifically, we discuss how IDPs may experience in vivo environments differently to ordered proteins. To this end, we provide a description of the compositional and physical parameters of the cellular milieu and their effects on ordered and disordered proteins (section 2). We evaluate how biological processes may act differently on ordered and disordered proteins (section 3) and discuss how combined physical and biological contributions modulate the intracellular aggregation behavior of IDPs (section 4). Finally, we review theoretical and experimental approaches to study the structural and functional properties of disordered proteins in cells (section 5)." @default.
• W2057567541 created "2016-06-24" @default.
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• W2057567541 date "2014-06-05" @default.
• W2057567541 modified "2023-10-16" @default.
• W2057567541 title "Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)" @default.
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