Myoglobin strikes back

被引：29

作者：

Brunori, Maurizio ^{[1
]}

机构：

[1] Univ Roma La Sapienza, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy

来源：

PROTEIN SCIENCE | 2010年 / 19卷 / 02期

关键词：

myoglobin; H-atom; molecular biology; protein science; CYTOCHROME-C-OXIDASE; 3-DIMENSIONAL FOURIER SYNTHESIS; SPERM-WHALE MYOGLOBIN; NITRIC-OXIDE; LIGAND-BINDING; STRUCTURAL DYNAMICS; X-RAY; MOLECULAR-DYNAMICS; CRYSTAL-STRUCTURE; CARBON-MONOXIDE;

D O I：

10.1002/pro.300

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Over the last half century, myoglobin (Mb) has been an excellent model system to test a number of concepts, theories, and new experimental methods that proved valuable to investigate protein structure, function, evolution, and dynamics. Mb's function, most often considered just an oxygen repository, has considerably diversified over the last 15 years, especially because it was shown to have a role in the biochemistry of quenching and synthesizing nitric oxide in the red muscle, thereby protecting the cell. To tackle protein's structural dynamics by innovative biophysical methods, Mb has been the best prototype; laser flash technology made it possible to obtain molecular movies by time-resolved Laue crystallography (with ps resolution). This approach unveiled the complexity of the energy landscape and the structural basis of the stretched interconversion between conformational substates of a protein.

引用

页码：195 / 201

页数：7

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