• 我要登录|
  • 免费注册
    |
  • 我的丁香通
    • 企业机构:
    • 成为企业机构
    • 个人用户:
    • 个人中心
  • 移动端
    移动端
丁香通 logo丁香实验_LOGO
搜实验

    大家都在搜

      大家都在搜

        0 人通过求购买到了急需的产品
        免费发布求购
        发布求购
        点赞
        收藏
        wx-share
        分享

        Structure-Function studies based on in vitro expression

        互联网

        603
        The advent of efficient procedures for site-directed and random in vitro mutagenesis has led to detailed exploration of protein structure-function relationships. Using these approaches, amino acid residues critical for protein activity can be determined in the absence of X-ray crystallographic data (1 , 2 ). An important prerequisite for any study examining protein structure-function relationships is an efficient expression system that gives not only adequate protein yield, but also fully native protein. Expression of mammalian genes in E. coli is often very successful with good protein yields, but some proteins are not correctly folded and, as a consequence, are not fully biologically active. Structure-function studies can be hampered by poor expression of modified proteins in both yeast and E. coli (3 ). Mammalian expression systems can give high-fidelity protein, but often the protein yield is poor and significant purification may be required. Systematic studies of protein using mutagenesis often require the analysis of a large number of modified proteins. If this process requires recloning into expression vectors, expression of protein, and purification, the analysis of a large number of proteins becomes prohibitive. The rabbit reticulocyte lysate (RRL,) translation system can be used to provide small quantities of protein when primed with synthetic mRNA generated in vitro from DNA templates with bacterial RNA polymerases.
        ad image
        提问
        扫一扫
        丁香实验小程序二维码
        实验小助手
        丁香实验公众号二维码
        扫码领资料
        反馈
        TOP
        打开小程序