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Showing 1 to 20 of 62 for “"Intrinsically disordered proteins"”.
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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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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
… challenging 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 …
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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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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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Intrinsic Disorder in Transcription Factors
… in nucleated 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 …
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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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Weighting protein ensembles with Bayesian statistics and small-angle X-ray scattering data
Intrinsically Disordered Proteins (IDPs) are involved in a number of neurodegenerative disorders such as Parkinson's and Alzheimer's diseases. Their disordered nature allows them to sample many different conformations, so their structures must be represented as ensembles. Typically, structural …
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Computational studies of tau protein : implications for the pathogenesis and treatment of neurodegenerative diseases
… it belongs to a class of heteropolymers known as intrinsically disordered proteins (IDPs). Unlike most proteins, IDPs adopt many distinct conformations under physiological conditions. In spite of their disordered nature, evidence exists that such proteins may exhibit residual structural …
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Regulation of E. coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products
… DNA polymerase V for mutagenic TLS. The small proteins UmuD2 and UmuD'2 make a large number of specific protein-protein contacts for their roles in regulation. This report chronicles experiments that indicate that umuD gene products share characteristics with intrinsically disordered proteins, …
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STRUCTURE-BASED APPROACHES TO DATA-DRIVEN PROTEIN FOLDING, AGGREGATION, AND SELF-ASSEMBLY
… protein folding, and the dynamics of intrinsically disordered proteins - remains a limitation of most approaches due to system size and sampling limitations. This work presents the development and application of the multi-eGO model, a data-driven, hybrid structure-based approach …
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Phosphoserine Incorporation into the Intrinsically Disordered N-terminal Domain of the p53 Tumor Suppressor Protein
… usually occurs within protein regions that are intrinsically disordered, quantitative and structural descriptions of phosphorylation effects in intrinsically disordered proteins (IDPs) are needed to understand the molecular basis of key aspects of development, aging, and disease. A few studies …
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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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Phase Separation Mediated Compartmentalisation of Rotavirus Replication
… and viral particle assembly in rotaviruses. Intrinsically disordered proteins are key drivers of LLPS. In rotaviruses, the disordered protein NSP5 binds the RNA chaperone NSP2, viral RNAs and other viral proteins to form replication factories known as viroplasms. Early in infection, these …
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Microfluidic Approaches for Investigating Aggregated Forms of Disease-Related Proteins
The self-assembly of soluble proteins is a common phenomenon observed in nature. It ranges from the formation of functional biomaterials, such as actin filaments and tubulin microtubules that form the cytoeskeleton, to the abnormal deposition of aberrant aggregates that lead to disease. There are …
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