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Showing 1 to 20 of 70 for “"Disordered proteins"”.
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Small Molecule Binding to Disordered Proteins
The human proteome includes many proteins that are entirely disordered or contain long disordered regions. Although these proteins are linked with many diseases, there are currently no clinically-approved drugs that have been shown to target these proteins in their monomeric forms. In fact, …
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Probing Order within Intrinsically Disordered Proteins
… understand the mechanisms behind how and why proteins fold, with natively unfolded proteins thought to be experimental artefacts. Today, the field of natively unfolded – or so-called intrinsically disordered – proteins, is rapidly developing. Protein disorder content has been positively …
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Intrinsically Disordered Proteins within the Genome
… code and permits the transcription of different proteins varying with cell lineages/cycles. The proteins that makeup, modify and read the chromatin structure are particularly enriched in `Intrinsic Disorder’ – a class of proteins lacking a well-defined structure but existing as a dynamic ensemble …
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Kinetics of Disordered Proteins and their Interactions
Disordered proteins and regions are highly prevalent in the human proteome, and are often implicated in disease. However, methods to study these systems in detail are lacking, and the potential for thermodynamic and kinetic characterisation using experimental methods is limited. Molecular …
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Decoding the Sequence-Dependent Properties of Intrinsically Disordered Proteins
… sequence-structure-function paradigm, whereby a proteins sequence codes for a specific structure that complements its binding partner, thus imparting functionality. Intrinsically disordered proteins (IDPs) lack a well-defined structure yet manage to interact with a variety of partners. At a basic …
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Intrinsically disordered proteins in molecular recognition and structural proteomics
Intrinsically disordered proteins (IDPs) are abundant in nature, being more prevalent in the proteomes of eukaryotes than those of bacteria or archaea. As introduced in Chapter I, these proteins, or portions of these proteins, lack stable equilibrium structures and instead have dynamic …
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Investigating Cold Adaptation of Intrinsically Disordered Proteins in p53 Homologs
No abstract prepared.
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An investigation of intrinsically disordered proteins in Gram-negative bacteria
… results in the production of small acid-soluble proteins (SASPs) to coat the spore DNA and shield it from UV radiation. While orthologs of these SASPs exist in many sporulating and non-sporulating bacteria, they are noticeably absent from the Gram-negative spore-forming Myxococcus xanthus. This …
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Modeling intrinsically disordered proteins ; a comprehensive study of [alpha]-synuclein
… to study because it is an Intrinsically Disordered Protein (IDP); i.e., it lacks a well-defined structure in aqueous solution. Unlike folded proteins, IDPs typically interconvert between many different conformations during their biological lifetime. In this thesis we apply novel methods …
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A Highly Charged Topic: Intrinsically Disordered Proteins and Protein pKa Values
Intrinsically disordered proteins (IDPs) are known not only for their roles in disease but also for their conformational flexibility, which makes them elusive for experimentation. We consider the role played by theory and simulation in resolving important questions pertaining to IDP structure and …
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Conformational Analysis of Disordered Proteins Using H/D Exchange Mass Spectrometry
Intrinsically disordered proteins (IDPs) represent a growing area of scientific interest. The prevalence of IDPs within the proteomes of complex organisms and the importance of these proteins in cellular functions has become apparent. The application of hydrogen/deuterium exchange mass spectrometry …
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Primary Structure and Solution Conditions Determine Conformational Ensemble Properties of Intrinsically Disordered Proteins
<p>Intrinsically disordered proteins (IDPs) are a class of proteins that do not exhibit well-defined three-dimensional structures. The absence of structure is intrinsic to their amino acid sequences, which are characterized by low hydrophobicity and high net charge per residue compared to folded …
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Uncovering the Roles and Evolved Sequence Grammar of Hypervariable Intrinsically Disordered Proteins in Bacterial Cell Division
… core. FtsZ has a bristled architecture, where a disordered tail, called the C-terminal tail (CTT), flanks the folded domain. The essentiality of the CTT was established through deletion experiments; however, the exact role that the CTT plays within the context of FtsZ function remained unclear. …
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Maximum Entropy Optimization: a General Approach to Study Ordered and Disordered Proteins Reveals Key Features of Protein Phase Separation
… However, the presence of both ordered and disordered domains in these proteins places a high demand on the model accuracy. In this thesis, we develop systematic methods to parameterize force fields from experimental data, and apply them to study the phase separation properties of chromatin …
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New experimental and theoretical tools for studying protein systems with elements of structural disorder
<p>Disordered proteins are one class of proteins which do not possess well-folded three-dimensional structures as their native conformations. Many eukaryotic proteins have been found to be fully disordered or contain certain disordered regions. Disordered proteins usually display several …
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Intrinsic Disorder in Transcription Factors
… cells. The major advantage of intrinsically disordered proteins or disordered regions is their inherent plasticity for molecular recognition, and this advantage promotes disordered proteins or disordered regions in binding their targets with high specificity and low affinity and with numerous …
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Programmable Assembly of Elastin-like Polypeptides Within Droplet Microenvironments
<p>Disordered proteins lack a defined secondary and higher order structure, possess a large number of biological functions, and are prevalent throughout nature. One important property of certain disordered proteins in biology is an ability to phase separate within the interior of a cell and form …
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Metabolism of Alpha-Synuclein by the 20S Proteasome
… The 20S proteasome is known to degrade proteins with regions of intrinsic disorder, which figure prominently in a wide range of neurodegenerative disorders, including alphaSyn in Parkinson's disease. Importantly, some forms of 20S exert an endoproteolytic activity that produces highly …
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Mechanisms of binding diversity in protein disorder : molecular recognition features mediating protein interaction networks
Intrinsically disordered proteins are proteins characterized by lack of stable tertiary structures under physiological conditions. Evidence shows that disordered proteins are not only highly involved in protein interactions, but also have the capability to associate with more than one partner. …
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