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Network of Conformational Transitions Revealed by Molecular Dynamics Simulations of the Carbonic Anhydrase II Apo-Enzyme

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成果类型:
期刊论文
作者:
Ma, Huishu;Li, Anbang;Gao, Kaifu*
通讯作者:
Gao, Kaifu
作者机构:
[Ma, Huishu; Gao, Kaifu; Li, Anbang] Cent China Normal Univ, Inst Biophys, Wuhan 430079, Hubei, Peoples R China.
[Ma, Huishu; Gao, Kaifu; Li, Anbang] Cent China Normal Univ, Dept Phys, Wuhan 430079, Hubei, Peoples R China.
通讯机构:
[Gao, Kaifu] C
Cent China Normal Univ, Inst Biophys, Wuhan 430079, Hubei, Peoples R China.
Cent China Normal Univ, Dept Phys, Wuhan 430079, Hubei, Peoples R China.
语种:
英文
期刊:
ACS OMEGA
ISSN:
2470-1343
年:
2017
卷:
2
期:
11
页码:
8414-8420
基金类别:
This work was supported by the National Natural Science Foundation of China under grant no. 11447013 as well as the self-determined research funds of CCNU from the college’s basic research and operation of MOE (grant nos. 23020205160030 and 20205170054).
机构署名:
本校为第一且通讯机构
院系归属:
物理科学与技术学院
心理学院
摘要:
Human carbonic anhydrase II (HCA II) is an enzyme that catalyzes the reversible hydration of CO 2 into bicarbonate (HCO 3 - ) and a proton (H + ) as well as other reactions at an extremely high rate. This enzyme plays fundamental roles in human physiology/pathology, such as controlling the pH level in cells and so on. However, the binding mechanism between apo-HCA II and CO 2 or other ligands as well as related conformational changes remains poorly understood, and atomic investigation into it could promote our understanding of related internal ...

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