Tag

Intrinsically Disordered Proteins

All articles tagged with #intrinsically disordered proteins

science-and-technology1 year ago•29 min saved

"Exploring the Dynamic Structures of the Human Intrinsically Disordered Proteome"

Researchers have made available simulation trajectories and conformational properties for over 28,000 intrinsically disordered regions (IDRs) of the human proteome, providing a comprehensive resource for studying these proteins. The data, which includes amino acid sequences, sequence features, and conformational properties, is accessible through an online database. Additionally, various tools and databases were utilized to gather information, and the availability of raw data to reproduce the results has been ensured. This extensive resource aims to advance the understanding of the conformational ensembles and functional implications of intrinsically disordered proteins.

via Nature.com|

#conformational-ensembles #data-availability #intrinsically-disordered-proteins

science-and-technology1 year ago•3 min saved

"Advancing Biomolecular Condensate Modeling with New Simulation Tool"

A team at the University of Massachusetts Amherst has developed a novel simulation tool, called HyRes-GPU, to accurately model phase separations mediated by intrinsically disordered proteins (IDPs), a crucial process in subcellular organization and various diseases. This tool fills a critical gap in computer simulation of IDP phase separation and provides insights into the molecular mechanisms of phase separation, with potential implications for therapeutic strategies in treating diseases associated with disordered proteins. The team's next step is to apply their findings to larger-scale simulations of more complex biomolecular mixtures.

via Phys.org|

#biomolecular-condensates #intrinsically-disordered-proteins #molecular-modeling

science-and-technology2 years ago•4 min saved

Delving into the Depths: Unraveling the Mysteries of the Nuclear Pore Complex

Scientists from the Max Planck Institute of Biophysics and Johannes Gutenberg University Mainz have made a breakthrough in understanding the structure and function of nuclear pores, which play a crucial role in safeguarding DNA and cellular transport. Using a combination of synthetic biology, fluorescence microscopy, and computer simulations, the researchers visualized the behavior of intrinsically disordered proteins (IDPs) within the nuclear pore complex. They discovered that these IDPs form a dynamic, spaghetti-like barrier that allows essential cellular factors to pass through while blocking viruses and other harmful pathogens. This new understanding could lead to the development of drugs or vaccines to prevent viral infections and promote healthy aging.

via SciTechDaily|

#cell-biology #cellular-transport #intrinsically-disordered-proteins