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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Membrane Environment Modulates the pK(a) Values of Transmembrane Helices
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Membrane Environment Modulates the pK(a) Values of Transmembrane Helices

机译：膜环境调节跨膜螺旋的pK（a）值

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In this work, we apply the recently developed constant pH molecular dynamics technique to study protonation equilibria of titratable side chains in the context of simple transmembrane (TM) helices and explore the effect of pH on their configurations in membrane bilayers. We observe that, despite a significant shift toward neutral states, considerable population of different side chains stay in the charged state that give rise to pK(a) values around 9.6 for Asp and Glu and 4.5 to 6 for His and Lys side chains, respectively. These charged states are highly stabilized by favorable interactions between head groups, water molecules, and the charged side chains that are facilitated by substantial changes in the configuration of the peptides. The pH dependent configurations and the measured pK(a) values are in good agreement with relatively recent solid state NMR measurements. Our results presented here demonstrate that all-atom constant pH molecular dynamics can be applied to membrane proteins and peptides to obtain reliable pK(a) values and pH dependent behavior for these systems.
机译：在这项工作中，我们应用了最近开发的恒定pH分子动力学技术，以研究在简单跨膜（TM）螺旋的情况下可滴定侧链的质子平衡，并探讨了pH对它们在膜双层中构型的影响。我们观察到，尽管向中性态有很大的转变，但相当数量的不同侧链仍处于带电状态，分别导致Asp和Glu的pK（a）值约为9.6，His和Lys侧链的pK（a）值分别为4.5至6 。这些电荷状态通过头基，水分子和带电侧链之间的有利相互作用而高度稳定，这些相互作用通过肽构型的显着改变而得以促进。 pH依赖的构型和测得的pK（a）值与相对较新的固态NMR测量非常吻合。我们在这里提出的结果证明，全原子恒定pH分子动力学可以应用于膜蛋白和肽，以获得可靠的pK（a）值和这些系统的pH依赖行为。

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