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Myoglobin strikes back
Author(s) -
Brunori Maurizio
Publication year - 2010
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.300
Subject(s) - myoglobin , protein dynamics , flash (photography) , quenching (fluorescence) , molecular dynamics , function (biology) , energy landscape , biological system , nitric oxide , chemistry , biophysics , nanotechnology , computer science , chemical physics , materials science , physics , biochemistry , computational chemistry , optics , biology , fluorescence , evolutionary biology , organic chemistry
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.