Solution structure of a BolA-like protein from Mus musculus

Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus.

The solution structure of the mouse pro-hormone convertase (PC) 1 pro-domain was determined using heteronuclear NMR spectroscopy and is the first structure to be obtained for any of the domains in the convertase family. The ensemble of NMR-derived structures shows a well-ordered core consisting of a four-stranded antiparallel beta-sheet with two alpha-helices packed against one side of this she...

X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus

The 2.07 A resolution X-ray crystal structure of a soluble Rieske-type ferredoxin from Mus musculus encoded by the gene Mm.266515 is reported. Although they are present as covalent domains in eukaryotic membrane oxidase complexes, soluble Rieske-type ferredoxins have not previously been observed in eukaryotes. The overall structure of the mouse Rieske-type ferredoxin is typical of this class of...

Leptospirosis in small mammals of Iran: II: Isolation of Leptospira grippotyphosa, from Mus musculus

Expanding the genetic code of Mus musculus

Here we report the expansion of the genetic code of Mus musculus with various unnatural amino acids including Nɛ-acetyl-lysine. Stable integration of transgenes encoding an engineered Nɛ-acetyl-lysyl-tRNA synthetase (AcKRS)/tRNAPyl pair into the mouse genome enables site-specific incorporation of unnatural amino acids into a target protein in response to the amber codon. We demonstrate temporal...

Ontogenesis of serum esterases in Mus musculus.

INTRODUCTION Electrophoretic techniques by which mixtures of isoenzymes, and homologous proteins generally, may be resolved have become valuable tools in developmental biology. They make possible the study of development at the molecular level, in the sense that the differentiation of protein patterns underlies ontogenetic changes and tissue differences. The greater successes of this approach h...