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The distance separating Cys-10 from the high-affinity metal binding site in actin.

作者信息

Miki M, Barden J A, dos Remedios C G

出版信息

Biochem Int. 1986 Jun;12(6):807-13.

PMID:3741444
Abstract

The fluorescence resonance energy transfer between 5-[2-[iodoacetyl)amino)ethyl]aminonaphthalene-1-sulphonic acid (1,5-IAEDANS) attached to Cys-10 residue and Co2+ bound to the high affinity metal site was measured. The resonance energy transfer efficiency was 8 +/- 2%, which corresponds to a distance of 2.1 nm using the absorption spectrum of Co-EDTA and 3.0 nm using the more relevant absorption spectrum of Co2+ bound to carboxypeptidase as a model spectrum of Co2+ bound to actin, respectively.

摘要

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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.