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重新审视冷冻电子显微镜下的血红蛋白和肌红蛋白结构。

Revisiting the Structure of Hemoglobin and Myoglobin with Cryo-Electron Microscopy.

机构信息

Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.

Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany.

出版信息

J Mol Biol. 2017 Aug 18;429(17):2611-2618. doi: 10.1016/j.jmb.2017.07.004. Epub 2017 Jul 8.

Abstract

Sixty years ago, the first protein structure of myoglobin was determined by John Kendrew and his colleagues; hemoglobin followed shortly thereafter. For quite some time, it seemed that only X-ray crystallography would be capable of determining the structure of proteins to high resolution. In recent years, cryo-electron microscopy has emerged as a viable alternative and indeed in many cases the preferred approach. It is capable of studying proteins that span a size range from several megadaltons to proteins as small as myoglobin and hemoglobin.

摘要

六十年前,约翰·肯德鲁(John Kendrew)及其同事首次确定了肌红蛋白的蛋白质结构;此后不久,血红蛋白的结构也被确定。在相当长的一段时间里,似乎只有 X 射线晶体学才能高分辨率地确定蛋白质的结构。近年来,冷冻电子显微镜已成为一种可行的替代方法,实际上在许多情况下,它是首选方法。它能够研究跨度从数兆道尔顿到像肌红蛋白和血红蛋白这样小的蛋白质的蛋白质。

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