The dynamic orientation of membrane-bound peptides:: Bridging simulations and experiments
The dynamic orientation of membrane-bound peptides:: Bridging simulations and experiments
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DOI：
10.1529/biophysj.107.113043
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发表时间：
2007-12-15
影响因子：
3.4
通讯作者：
Salgado, Jesus
中科院分区：
文献类型：
--
作者：
Esteban-Martin, Santi;Salgado, Jesus
肽/膜超分子复合物中的结构组织最好由肽取向加上其时间依赖性和空间波动的知识来描述。由肽倾斜和围绕其分子轴的旋转定义的静态取向可以通过许多光谱方法获得。然而，肽动力学，虽然相关的了解这些系统的功能，仍然在很大程度上未被探索。在这里，我们描述的方向和动力学的色氨酸侧翼和赖氨酸侧翼的疏水肽在脂质双层分子动力学模拟。揭示了一种新的观点，集体的非平凡分布的时间演变和合奏肽的方向密切代表系统的实验研究。这样的全球分布是广泛的，揭示了存在的取向状态，这取决于锚定模式的界面残基。我们表明，这种动态调制H-2四极分裂，并介绍了在NMR数据分析的模糊性。这些发现表明，肽/膜复合物的结构描述是不完整的，在没有动力学知识的情况下，甚至是不精确的。
The structural organization in a peptide/membrane supramolecular complex is best described by knowledge of the peptide orientation plus its time-dependent and spatial fluctuations. The static orientation, defined by the peptide tilt and a rotation about its molecular axis, is accessible through a number of spectroscopic methods. However, peptide dynamics, although relevant to understand the functionality of these systems, remains largely unexplored. Here, we describe the orientation and dynamics of Trp-flanked and Lys-flanked hydrophobic peptides in a lipid bilayer from molecular dynamics simulations. A novel view is revealed, where collective nontrivial distributions of time-evolving and ensemble peptide orientations closely represent the systems as studied experimentally. Such global distributions are broad and unveil the existence of orientational states, which depend on the anchoring mode of interfacial residues. We show that this dynamics modulates H-2 quadrupolar splittings and introduces ambiguity in the analysis of NMR data. These findings demonstrate that structural descriptions of peptide/membrane complexes are incomplete, and in cases even imprecise, without knowledge of dynamics.