Autor: Steven Yun, Kush Dalal, Weiping Shen, Bonny Tam, Frederic Pio
Rok vydání: 2005
Předmět:
Zdroj: Proteome Science. 3:3
ISSN: 1477-5956
DOI: 10.1186/1477-5956-3-3
Popis: Background Protein expression in E. coli is the most commonly used system to produce protein for structural studies, because it is fast and inexpensive and can produce large quantity of proteins. However, when proteins from other species such as mammalian are produced in this system, problems of protein expression and solubility arise [1]. Structural genomics project are currently investigating proteomics pipelines that would produce sufficient quantities of recombinant proteins for structural studies of protein complexes. To investigate how the E. coli protein expression system could be used for this purpose, we purified apoptotic binary protein complexes formed between members of the Caspase Associated Recruitment Domain (CARD) family.
Databáze: OpenAIRE