The recent findings of Waldo et al. 1 demonstrate that the fusion of the green fluorescent protein (GFP) to insoluble proteins dramatically reduces its folding ability in prokaryotic cells.

Avoid fusions to the GFP fragments at the site of protein-protein interaction and consider optimizing the spacer length between the fusions and GFP fragments, if necessary. In the absence of ...

This study reveals a novel bioactive polycysteine polymer with high quantum yield and multicolor emission, showing promise ...

This valuable study reports the first characterization of the CG14545 gene in Drosophila melanogaster, which the authors name "Sakura." Acting during germline stem cell fate and differentiation, ...

Dynamic, reversible modifications of DNA and RNA regulate how genes are expressed and transcribed, which can influence ...

Jackson ImmunoResearch, a manufacturer of secondary antibodies and immunoreagents for the life science market, announces a ...

Synthetic variants of a green fluorescent protein To demonstrate the performance of ESM3, the start-up had the language model design synthetic variants of the green fluorescent protein (GFP ...

Explore ESM3's groundbreaking AI technology in protein design, offering new possibilities in drug discovery and material ...

RNAs have been shown to have a function in protein secretion after thousands more binding targets were identified using a ...