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肌动蛋白中酪氨酸-69与高亲和力核苷酸及金属结合位点之间的距离。

The distances separating Tyr-69 from the high-affinity nucleotide and metal binding sites in actin.

作者信息

Barden J A, Miki M

出版信息

Biochem Int. 1986 Feb;12(2):321-9.

PMID:3964288
Abstract

The nucleotide binding site in actin was occupied with the fluorescent analogue formycin A 5' triphosphate which acted as a fluorescent donor for the acceptor chromophore dansyl chloride attached to Tyr-69. The distance separating the two chromophores was calculated to be 2.1 nm from the fluorescence energy transfer measurements. Similar measurements were made of the distances separating dansyl chloride, acting as donor, on Tyr-69 from Co2+ occupying the metal binding site. A distance of 2.1 nm was similarly obtained.

摘要

肌动蛋白中的核苷酸结合位点被荧光类似物嘌呤霉素A 5'三磷酸占据,它作为荧光供体,为连接在Tyr-69上的受体发色团丹磺酰氯提供能量。通过荧光能量转移测量计算得出,两个发色团之间的距离为2.1纳米。对占据金属结合位点的Co2+与Tyr-69上作为供体的丹磺酰氯之间的距离进行了类似测量,同样得到了2.1纳米的距离。

相似文献

1
The distances separating Tyr-69 from the high-affinity nucleotide and metal binding sites in actin.肌动蛋白中酪氨酸-69与高亲和力核苷酸及金属结合位点之间的距离。
Biochem Int. 1986 Feb;12(2):321-9.
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引用本文的文献

1
Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation.肌动蛋白和肌球蛋白中距离的荧光共振能量转移测量:批判性评估
J Muscle Res Cell Motil. 1987 Apr;8(2):97-117. doi: 10.1007/BF01753986.
2
Structure of actin observed by fluorescence resonance energy transfer spectroscopy.通过荧光共振能量转移光谱法观察到的肌动蛋白结构。
J Muscle Res Cell Motil. 1992 Apr;13(2):132-45. doi: 10.1007/BF01874150.