Conventional NMR approaches to detect weak protein binding and aggregation are hindered by the increased viscosity brought about by crowding. We describe a simple and reliable NMR method to distinguish viscosity effects from binding and aggregation under crowded conditions
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. R...
Nuclear magnetic resonance (NMR) is amongst the most powerful and versatile spectroscopic tools for ...
In all intracellular processes, protein structure and dynamics are subjected to the influence of mac...
Conventional NMR approaches to detect weak protein binding and aggregation are hindered by the incre...
The cytoplasm is crowded, and the concentration of macromolecules can reach ~ 300 g/L, an environmen...
Most proteins function in nature under crowded conditions, and crowding can change protein propertie...
Despite increased attention, little is known about how the crowded intracellular environment affects...
In-cell NMR provides a valuable means to assess how macromolecules, with concentrations up to 300 g/...
In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions co...
Protein protein interaction is the fundamental step of biological signal transduction. Interacting p...
Molecular crowding occurs when the total concentration of macromolecular species in a solution is s...
We present an NMR method based on natural abundance 17O relaxation of water to determine effective v...
Macromolecular crowding has been shown by previous research to affect the stability of proteins. How...
Intrinsically disordered proteins are important in signaling, regulation, and translocation. Underst...
In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiolo...
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. R...
Nuclear magnetic resonance (NMR) is amongst the most powerful and versatile spectroscopic tools for ...
In all intracellular processes, protein structure and dynamics are subjected to the influence of mac...
Conventional NMR approaches to detect weak protein binding and aggregation are hindered by the incre...
The cytoplasm is crowded, and the concentration of macromolecules can reach ~ 300 g/L, an environmen...
Most proteins function in nature under crowded conditions, and crowding can change protein propertie...
Despite increased attention, little is known about how the crowded intracellular environment affects...
In-cell NMR provides a valuable means to assess how macromolecules, with concentrations up to 300 g/...
In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions co...
Protein protein interaction is the fundamental step of biological signal transduction. Interacting p...
Molecular crowding occurs when the total concentration of macromolecular species in a solution is s...
We present an NMR method based on natural abundance 17O relaxation of water to determine effective v...
Macromolecular crowding has been shown by previous research to affect the stability of proteins. How...
Intrinsically disordered proteins are important in signaling, regulation, and translocation. Underst...
In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiolo...
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human diseases. R...
Nuclear magnetic resonance (NMR) is amongst the most powerful and versatile spectroscopic tools for ...
In all intracellular processes, protein structure and dynamics are subjected to the influence of mac...
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