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- W2095729147 abstract "Intrinsically disordered proteins (IDPs) are increasingly recognized for their important roles in a range of biological contexts, both in normal physiological function and in a variety of devastating human diseases. However, their structural characterization by traditional biophysical methods, for the purposes of understanding their function and dysfunction, has proved challenging. Here, we investigate the model IDPs α-Synuclein (αS) and tau, that are involved in major neurodegenerative conditions including Parkinson’s and Alzheimer’s diseases, using excluded volume Monte Carlo simulations constrained by pairwise distance distributions from single-molecule fluorescence measurements. Using this, to our knowledge, novel approach we find that a relatively small number of intermolecular distance constraints are sufficient to accurately determine the dimensions and polymer conformational statistics of αS and tau in solution. Moreover, this method can detect local changes in αS and tau conformations that correlate with enhanced aggregation. Constrained Monte Carlo simulations produce ensembles that are in excellent agreement both with experimental measurements on αS and tau and with all-atom, explicit solvent molecular dynamics simulations of αS, with much lower configurational sampling requirements and computational expense." @default.
- W2095729147 created "2016-06-24" @default.
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- W2095729147 date "2012-11-01" @default.
- W2095729147 modified "2023-10-18" @default.
- W2095729147 title "The Conformational Ensembles of α-Synuclein and Tau: Combining Single-Molecule FRET and Simulations" @default.
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- W2095729147 doi "https://doi.org/10.1016/j.bpj.2012.09.032" @default.
- W2095729147 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3491709" @default.
- W2095729147 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23199922" @default.
- W2095729147 hasPublicationYear "2012" @default.
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