人硫氧还蛋白是单体还是二聚体？
Is human thioredoxin monomeric or dimeric?
作者信息
Gronenborn A M, Clore G M, Louis J M, Wingfield P T
机构信息
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
出版信息
Protein Sci. 1999 Feb;8(2):426-9. doi: 10.1110/ps.8.2.426.
Abstract
We have examined the molecular weight and rotational correlation time of human thioredoxin by analytical ultracentrifugation and NMR spectroscopy, respectively. Two variants of human thioredoxin were studied, namely human thioredoxin identical in amino acid sequence to the one whose NMR structure we previously determined (C62A, C69A, C73A, M74T) and human thioredoxin (C62A, C69A, C73A, M74) containing the wild-type amino acid methionine at position 74. In both cases, the experimental data indicate that the predominant species is monomeric and we find no evidence for the existence of a well-defined dimeric form as was observed in the recently reported crystal structure (Weichsel et al., 1996) of human thioredoxin and the C73S mutant.
摘要
我们分别通过分析超速离心和核磁共振光谱法研究了人硫氧还蛋白的分子量和旋转相关时间。研究了人硫氧还蛋白的两种变体，即氨基酸序列与人硫氧还蛋白（C62A、C69A、C73A、M74T）相同，其核磁共振结构我们之前已确定，以及人硫氧还蛋白（C62A、C69A、C73A、M74），其第74位含有野生型氨基酸甲硫氨酸。在这两种情况下，实验数据均表明主要形式为单体，并且我们没有发现存在如最近报道的人硫氧还蛋白和C73S突变体的晶体结构（Weichsel等人，1996年）中所观察到的明确二聚体形式的证据。
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