Isolation, separation and purification articles from across Nature Portfolio

A unique soluble β-carotene-binding protein pigment extracted from yellow locust cuticle is biochemically and spectroscopically equivalent to the protein reconstituted in carotenoid-producing E. coli cells and capable of binding to chitin in vitro.

The authors present a method utilizing the reversible protein tag ProMTag to prepare high-quality, sequencing-ready DNA and RNA, and either intact proteins or mass spectrometry-ready peptides for whole proteome analysis from a single sample.

Scientific research on human insulin was a crucial development in medicine, and its discovery led to the treatment of diabetes, one of the most prevalent global chronic diseases. A seminal work published in 1979 describing recombinant DNA technology to produce human insulin through biocatalysis has resulted in this field’s establishment and routine industrial applications.

Constructing aptamers with desired target-binding affinities may lead to new applications but is challenging. Now, a new method using a high-dimensional microfluidic approach enables quantitative isolation of aptamers with programable binding affinities.

Hyperfolder yellow fluorescent protein (hfYFP) and its variants are fluorescent proteins with high chemical and thermal stability. They resist aggregation, withstand diverse chemical challenges and show promise in expansion and electron microscopies. The chloride resistance and uncanny stability in guanidinium of hfYFP enable fluorescence-guided protein purification under denaturing conditions.

Cancer cells frequently amplify oncogenes on DNA molecules outside of chromosomes — extrachromosomal DNA. A technique adapted for isolation of extrachromosomal DNA, termed CRISPR-CATCH, enables analyses of its genetic and epigenetic compositions, which provides insights into its origin, structural diversity and mechanism of oncogene activation in cancer.

Jijumon et al. introduce a straightforward, cell-free assay to unravel the functions of microtubule-associated proteins.