Journal:Acta Cryst D:S2059798320013510
From Proteopedia
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In the present work, the refinement of the JK-loop is obatined for the first time by X-ray diffraction experiment, thanks to its crystal packing mode. To support the X-ray observation, Molecular Dynamics trajectories are also carried out to provide a dynamical information about the loop in the presence of the cofactor. Such new structural and dynamical information highlights the importance of the JK-loop in confining the labile heme cofactor into the active site. | In the present work, the refinement of the JK-loop is obatined for the first time by X-ray diffraction experiment, thanks to its crystal packing mode. To support the X-ray observation, Molecular Dynamics trajectories are also carried out to provide a dynamical information about the loop in the presence of the cofactor. Such new structural and dynamical information highlights the importance of the JK-loop in confining the labile heme cofactor into the active site. | ||
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<b>References</b><br> | <b>References</b><br> | ||
Revision as of 15:30, 21 October 2020
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