Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics.
Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics.
复制标题
糖基化和拥挤膜对流感神经氨酸酶稳定性和动力学的影响。
DOI：
10.1101/2023.09.10.556910
复制
发表时间：
2023
期刊：
影响因子：
--
通讯作者：
McCammon,JAndrew
中科院分区：
文献类型：
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作者：
Seitz,Christian;Deveci,İlker;McCammon,JAndrew
All protein simulations are conducted with varying degrees of simplification, oftentimes with unknown ramifications about how these simplifications affect the interpretability of the results. In this work, we investigated how protein glycosylation and lateral crowding effects modulate an array of properties characterizing the stability and dynamics of influenza neuraminidase. We constructed three systems: (1) glycosylated neuraminidase in a whole virion (i.e., crowded membrane) environment, (2) glycosylated neuraminidase in its own lipid bilayer, and (3) unglycosylated neuraminidase in its own lipid bilayer. We saw that glycans tend to stabilize the protein structure and reduce its conformational flexibility while restricting the solvent movement. Conversely, a crowded membrane environment encouraged exploration of the free energy landscape and a large-scale conformational change, while making the protein structure more compact. Understanding these effects informs what factors one must consider in attempting to recapture the desired level of physical accuracy.
