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文献和实验Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli
Escherichia coli has traditionally been a popular host for the production of heterologous proteins because of its ease of genetic manipulation and growth. Recombinant proteins produced in E. coli have been useful for a variety of purposes
Protein Modification to Probe Intradynein Interactions and In Vivo Redox State
interactions involving dynein components by chemical cross-linking and a recently developed technique to assess the in vivo redox state of thioredoxin-like proteins that are associated with axonemal dyneins from a wide range of organisms. Finally
The completion of the human genome project has ushered in a new era of life science (1 ,2 ) in which the new challenge is to understand functions of the entire collection of the gene products, or the proteome. One important feature
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