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Articles by Benjamin Schuler
Phosphorylation tunes electrostatically driven protein-RNA interactions
Abstract Phosphorylation of intrinsically disordered proteins (IDPs) regulates many biomolecular interactions, yet its quantitative effects on binding of highly charged IDPs to nucleic acids remain unclear. Here, we show that multi-site phosphorylation of the disordered arginine/serine-rich (RS) domain of the splicing factor SRSF1 functions as an electrostatic rheostat controlling RNA binding.
Toward a unified framework for determining conformational ensembles of disordered proteins - Nature Methods
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Abstract Disordered proteins play essential roles in myriad cellular processes, yet their structural characterization remains a major challenge due to their dynamic and heterogeneous nature. Here we present a community-driven initiative to address this problem by advocating a unified framework for determining conformational ensembles of disordered proteins.
By Hamidreza Ghafouri, Pavel Kadeřávek, Ana Melo, Maria Cristina Aspromonte, Pau Bernadó, Juan Manuel Cortes, Juan Cortés Verified, Zsuzsanna Dosztanyi, Michael Feig, Giacomo Janson, Kresten Lindorff-Larsen, Peter Nagy, Péter R. Nagy, Richard G. Pestell, Damiano Piovesan, Marco Schiavina, Benjamin Schuler, Nathalie Sibille, Giulio Tesei, Peter Tompa, Michele Vendruscolo, Jiri Vondrasek, Wim Vranken, Alexander Miguel Monzon, Frans A. A. Mulder, Lukas Zidek, Silvio C. E. Tosatto
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Nature
Verified
The molecular basis of lamin-specific chromatin interactions - Nature Structural & Molecular Biology
Abstract In the cell nucleus, chromatin is anchored to the nuclear lamina, a network of lamin filaments and binding proteins that underly the inner nuclear membrane. The nuclear lamina is involved in chromatin organization through the interaction of lamina-associated domains within the densely packed heterochromatin regions.
Role of charges in a dynamic disordered complex between an IDP and a folded domain - Nature Communications
Abstract Protein complexes involving intrinsically disordered proteins (IDPs) cover a continuum from IDPs that fully fold upon binding to IDPs that remain fully disordered in the complex. Here we demonstrate a case of charge-driven interactions of a folded domain with an oppositely charged IDP that remains completely disordered in the complex.
Stereochemistry in the disorder–order continuum of protein interactions - Nature
Abstract Intrinsically disordered proteins can bind via the formation of highly disordered protein complexes without the formation of three-dimensional structure1. Most naturally occurring proteins are levorotatory (l)—that is, made up only of l-amino acids—imprinting molecular structure and communication with stereochemistry2. By contrast, their mirror-image dextrorotatory (d)-amino acids are rare in nature.
Single-Molecule FRET at 10 MHz Count Rates
Abstract A bottleneck in many studies utilizing single-molecule Forster Resonance Energy Transfer (smFRET) is the attainable photon count rate as it determines the temporal resolution of the experiment. As many biologically relevant processes occur on timescales that are hardly accessible with currently achievable photon count rates, there has been considerable effort to find strategies to increase the stability and brightness of fluorescent dyes.
Single-Molecule FRET at 10 MHz Count Rates
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Am. Chem. Soc. 2024, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
Impact of In‐Cell and In‐Vitro Crowding on the Conformations and Dynamics of an Intrinsically Disordered Protein
Research Article Prof. Dr. Andrea Soranno Corresponding Author soranno@wustl.edu Department of Biochemistry and Molecular Biophysics, Center for Science and Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, USA Search for more papers by this author PDF ShareShare Abstract The conformations and dynamics of proteins can be influenced by crowding from the large concentrations of macromolecules within cells.
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study - Nature Methods
Nomenclature and definitions See Supplementary Table 5 for a summary of the following section. The FRET efficiency E is defined as $$E = \frac{{F_{\rm{A|D}}}}{{F_{\rm{D|D}} + F_{\rm{A|D}}}}$$ (1) where F is the signal.
A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction
All protein sequences used in this study are compiled in Supplementary Table 3. All primers (Microsynth) used for site-directed mutagenesis are listed in Supplementary Table 4. The coding sequences of Avi-tagged single-cysteine NCBD and ACTR variants for immobilization were cloned via BamHI/HindIII into a pAT222-pD expression vector (gift of J. Schöppe and A. Plückthun)54, yielding an expression construct with an N-terminal Avi-tag and a Thrombin-cleavable C-terminal His -tag.
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