Structural and mutational analysis of a monomeric and dimeric form of a single domain antibody with implications for protein misfolding
Structural and mutational analysis of a monomeric and dimeric form of a single domain antibody with implications for protein misfolding
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DOI：
10.1002/prot.24671
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发表时间：
2014-11-01
影响因子：
2.9
通讯作者：
Legler, Patricia M.
中科院分区：
文献类型：
--
作者：
George, Jade;Compton, Jaimee R.;Legler, Patricia M.
骆驼科单结构域抗体（sdAb）以其热稳定性和可逆重折叠而闻名。我们已经表征了一种异常稳定的sdAb，其识别葡萄球菌肠毒素B，具有所报道的最高解链温度之一（Tm =85 ℃）。出乎意料的是，大约10-20%的蛋白质在溶液中形成二聚体。另外三起案件
Camelid single domain antibodies (sdAb) are known for their thermal stability and reversible refolding. We have characterized an unusually stable sdAb recognizing Staphylococcal enterotoxin B with one of the highest reported melting temperatures (T-m=85 degrees C). Unexpectedly, approximate to 10-20% of the protein formed a dimer in solution. Three other cases where