Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants
Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants
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DOI：
10.1002/pro.5560060819
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发表时间：
1997-08-01
期刊：
影响因子：
8
通讯作者：
Mayo, SL
中科院分区：
文献类型：
--
作者：
Morgan, CS;Holton, JM;Mayo, SL
I类主要组织相容性复合体（MHC）分子结合来自降解蛋白的肽，用于展示给免疫系统的T细胞。肽以不同的亲和力与MHC蛋白结合，这取决于它们的序列和长度。我们证明了MHC-肽复合物的热稳定性直接取决于肽结合亲和力。我们使用这种相关性开发一种方便的方法来确定肽解离常数通过测量MHC-肽复合物的稳定性，使用热变性配置文件监测圆二色性。
Class I major histocompatibility complex (MHC) molecules bind peptides derived from degraded proteins for display to T cells of the immune system. Peptides bind to MHC proteins with varying affinities, depending upon their sequence and length. We demonstrate that the thermal stability of the MHC-peptide complex depends directly on peptide binding affinity. We use this correlation to develop a convenient method to determine peptide dissociation constants by measuring MHC-peptide complex stability using thermal denaturation profiles monitored by circular dichroism.