Many of the features of Crazy Horse's personal appearance appear correct - one feather, long loose hair, breechclout, and hail stones painted on his naked, otherwise unadorned body - but Crazy Horse did not paint his body yellow and there is no lightning flash painted on Crazy Horse's face. So the depiction of Crazy Horse shooting at full charge is doubtful. And He Dog said that Crazy Horse was the only Indian he ever knew who almost always dismounted to shoot. For instance, Flying Hawk recalled how Crazy Horse personally rode among the American soldiers and " killed a lot of them with his war-club" - not his rifle. This drawing was done decades later from stories by tribal elders, like his uncle He Dog, and it is inaccurate in some respects. Although he was present at the battle, Amos Bad Heart Bull was only seven years old at the time and did not actually witness Crazy Horse in action. THIS DETAIL from a pictograph by Amos Bad Heart Bull depicts Crazy Horse at the Battle of the Little Bighorn. Atrocities * Indian Atrocitiesįeatures: Little Bighorn Mysteries * Virtual Museum Guided Tours: Crazy Horse at the Little Bighorn * Crazy Horse at the Rosebudįeatures: Who Killed Custer? * Who Killed Custer? Audio Bookįeatures: Crazy Horse Surrender Ledger * Winter Count of Crazy Horse's Lifeįeatures: Bogus Crazy Horse Photos * Unsung 7th Cavalry Scouts Sagaįeatures: Indian Battlefield Tactics * Woman Warriors * Little Bighorn Mapsįeatures: U.S. The conservation of this structural feature and its close proximity to the heme iron atom strongly implicate this internal water molecule as having a functional role in the mechanism of action of cytochrome c.ĭepartment of Biochemistry, University of British Columbia, Vancouver, Canada.100 Voices: Full List * Crow/Arikara * Sioux/Cheyenne * American * Rosebud It is shown that this latter water molecule shifts in a consistent manner upon change in oxidation state if cytochrome c structures from various sources are compared. The other is more centrally buried near the heme iron atom and is hydrogen bonded to the conserved residues Asn52, Tyr67 and Thr78. One of these mediates a charged interaction between the invariant residue Arg38 and a nearby heme propionate. The remaining two are internally located. Three of these are on the surface of the protein, serving to stabilize local polypeptide chain conformations. In total, five water molecules occupy conserved positions in the structures of horse heart, yeast iso-1, tuna and rice cytochromes c. The positioning of this residue does not therefore appear to be oxidation-state-dependent. This study also demonstrates that, in horse cytochrome c, the side-chain of Phe82 is positioned in a co-planar fashion next to the heme in a conformation comparable to that found in other cytochromes c. The first of these variable regions is part of a surface beta-loop, whilst the latter two are located together adjacent to the heme group. Significant conformational differences between these proteins occur in three regions and primarily involve residues 22 to 27, 41 to 43 and 56 to 57. A comprehensive analysis of the structural differences between horse heart cytochrome c and those other eukaryotic cytochromes c for which high-resolution structures are available (yeast iso-1, tuna, rice) has also been completed. This has allowed for a detailed assessment of the structural features of this protein, including the presence of secondary structure, hydrogen-bonding patterns and heme geometry. The 1.94 A resolution three-dimensional structure of oxidized horse heart cytochrome c has been elucidated and refined to a final R-factor of 0.17. Diversity, Equity, Inclusion, and Access.Citation, Usage, Privacy Policies, Logo.Biologically Interesting Molecule Reference Dictionary (BIRD).
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