Protein 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.

Structural and functional analysis of human proteins requires their isolation in high yields and purity. Here, protease-cleavable, high-affinity, tag-specific nanobodies are used for the isolation of soluble and membrane proteins from lentiviral-transduced human cell suspensions.

Purifying proteins by crystallization rather than chromatography is less expensive and more environmentally sustainable. This protocol describes how to determine the operational conditions for purifying monoclonal antibodies by template-assisted membrane crystallization.

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.

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.