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2
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I类主要组织相容性复合体-肽平衡解离常数的圆二色性测定

Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants.

作者信息

Morgan C S, Holton J M, Olafson B D, Bjorkman P J, Mayo S L

机构信息

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.

出版信息

Protein Sci. 1997 Aug;6(8):1771-3. doi: 10.1002/pro.5560060819.

DOI:10.1002/pro.5560060819
PMID:9260291
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143769/
Abstract

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.

摘要

I类主要组织相容性复合体（MHC）分子结合源自降解蛋白质的肽段，以供免疫系统的T细胞识别。肽段与MHC蛋白的结合亲和力各不相同，这取决于它们的序列和长度。我们证明，MHC-肽复合物的热稳定性直接取决于肽段的结合亲和力。我们利用这种相关性开发了一种简便方法，通过使用圆二色性监测的热变性曲线来测量MHC-肽复合物的稳定性，从而确定肽段的解离常数。