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首页> 外文期刊>Biophysical Journal >Flow-induced beta-hairpin folding of the glycoprotein Ibalpha beta-switch.
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Flow-induced beta-hairpin folding of the glycoprotein Ibalpha beta-switch.

机译：流诱导的糖蛋白Ibalpha beta开关的beta发夹折叠。

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摘要

Flow-induced shear has been identified as a regulatory driving force in blood clotting. Shear induces beta-hairpin folding of the glycoprotein Ibalpha beta-switch which increases affinity for binding to the von Willebrand factor, a key step in blood clot formation and wound healing. Through 2.1-micros molecular dynamics simulations, we investigate the kinetics of flow-induced beta-hairpin folding. Simulations sampling different flow velocities reveal that under flow, beta-hairpin folding is initiated by hydrophobic collapse, followed by interstrand hydrogen-bond formation and turn formation. Adaptive biasing force simulations are employed to determine the free energy required for extending the unfolded beta-switch from a loop to an elongated state. Lattice and freely jointed chain models illustrate how the folding rate depends on the entropic and enthalpic energy, the latter controlled by flow. The results reveal that the free energy landscape of the beta-switch has two stable conformations imprinted on it, namely, loop and hairpin--with flow inducing a transition between the two.
机译：流动引起的剪切已被鉴定为血液凝固中的调节驱动力。剪切诱导糖蛋白Ibalphaβ-开关的β-发夹折叠，从而增加与von Willebrand因子结合的亲和力，这是血凝块形成和伤口愈合的关键步骤。通过2.1微米分子动力学模拟，我们研究了流动诱导的β-发夹折叠的动力学。对不同流速进行采样的模拟显示，在流动下，β-发夹折叠是由疏水性塌陷引发的，随后是链间氢键形成和转向形成。自适应偏压力模拟用于确定将展开的β开关从环延伸到拉长状态所需的自由能。晶格和自由连接的链模型说明了折叠速率如何取决于熵和焓能量，后者由流量控制。结果表明，β-开关的自由能态具有两个稳定构象，即环和发夹-流动导致两者之间发生过渡。

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