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The team captured molecular ‘snapshots’ of RNF216 as it assembled chains of the small protein ubiquitin, which tags the target proteins to modify their behaviour in the cell.
The inset shows the molecular and chemical structure of the protein, miRFP718nano. [Junjie Yao, Duke University] Imaging deep tissues with light is challenging.
A newly designed small fluorescent protein that emits and absorbs light that penetrates deep into biological tissue can help researchers capture deeper, cleaner and more precise biomedical images. ...
More information: Ankur Garg et al, The structural landscape of Microprocessor-mediated processing of pri-let-7 miRNAs, Molecular Cell (2024). DOI: 10.1016/j.molcel.2024.09.008 Provided by Cold ...
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Molecular messenger of sight: Scientists investigate protein structure RBP3's role in vision - MSNRetinol-binding protein 3 (RBP3) is a glycoprotein of about 140 kDa, found in the intercellular space of the retina. It plays an important role in the transport of retinoids—molecules essential ...
When proteins are made in a cell, they start out as strings of amino acids, which have to be folded into the correct, 3D ...
Single-protein imaging shows that the Pol IV DNA repair protein (red) moves along the DNA strand (green) with the complex that copies DNA (replisome). Credit: Tuan Pham, UC Davis “To use the analogy ...
Researchers found a rare example of an ancient protein that can still function in a molecular mirror world – offering new clues about the evolutionary history of proteins that bind to nucleic acids.
"The scale at which we analyzed the amyloid peptides was unprecedented," said Ben Lehner of the Wellcome Sanger Institute.
A new method for measuring the degree of protein labeling improves the quantitative analysis of microscopy images. genprowebdirectory Facebook Linkedin RSS Twitter Youtube ...
Biomedical and genetic engineers at Duke University and the Albert Einstein College of Medicine have designed a small fluorescent protein that emits and absorbs light that penetrates deep into ...
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