1bzp: Difference between revisions

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[[Image:1bzp.gif|left|200px]]
{{Seed}}
[[Image:1bzp.png|left|200px]]


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{{STRUCTURE_1bzp|  PDB=1bzp  |  SCENE=  }}  
{{STRUCTURE_1bzp|  PDB=1bzp  |  SCENE=  }}  


'''ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE'''
===ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE===




==Overview==
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The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide.
The line below this paragraph, {{ABSTRACT_PUBMED_10205052}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_10205052}}


==About this Structure==
==About this Structure==
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[[Category: Atomic resolution]]
[[Category: Atomic resolution]]
[[Category: Deoxy myoglobin]]
[[Category: Deoxy myoglobin]]
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