% of this molecule is in an alpha-helical secondary structure, and it exhibits a single hydrophobic cleft which contains an important metal prosthetic group as well as a histidine R group above the plane of its central ring. The first protein ever viewed in three dimensions by X-ray crystallography, it is common in the slow-twitch muscle fibers and is released into the bloodstream when a muscle is damaged, and thus a test for it can confirm muscle injury. The changing af
% of this molecule is in an alpha-helical secondary structure, and it exhibits a single hydrophobic cleft which contains an important metal prosthetic group as well as a histidine R group above the plane of its central ring. The first protein ever viewed in three dimensions by X-ray crystallography, it is common in the slow-twitch muscle fibers and is released into the bloodstream when a muscle is damaged, and thus a test for it can confirm muscle injury. The changing affinity for water in this molecule's reduced iron atom governs the changing color of meat. FTP, name this molecule, particularly common in the dark red tissues of diving mammals, which stores oxygen within cells rather than moving it through the blood like its counterpart, hemoglobin.
% of this molecule is in an alpha-helical secondary structure, and it exhibits a single hydrophobic cleft which contains an important metal prosthetic group as well as a histidine R group above the plane of its central ring.
myoglobin