The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form
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The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form Descriptor: A1 globin chain of giant V2 hemoglobin, A2 globin chain of giant V2 hemoglobin, B1 globin chain of giant V2 hemoglobin, ... Authors: Numoto, N, Nakagawa, T, Ohara, R, Hasegawa, T, Kita, A, Yoshida, T, Maruyama, T, Imai, K, Fukumori, Y, Miki, K. Deposit date: 2013-06-01 Release date: 2014-06-04 Last modified: 2024-11-13 Method: X-RAY DIFFRACTION (2.5 Å) Cite: The structure of a deoxygenated 400 kDa haemoglobin reveals ternary- and quaternary-structural changes of giant haemoglobins Acta Crystallogr.,Sect.D, 70, 2014
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2013-06-01
