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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Kinetically Trapped Liquid-State Conformers of a Sodiated Model Peptide Observed in the Gas Phase
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Kinetically Trapped Liquid-State Conformers of a Sodiated Model Peptide Observed in the Gas Phase

机译：在气相中观察到的化学模型肽的动力学捕获的液态整体剂

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摘要

We investigate the peptide AcPheAla(5)Lyar(+), a model system for studying helix formation in the gas phase, in order to fully understand the forces that stabilize the helical structure. In particular, we address the question of whether the local fixation of the positive charge at the peptide's C-terminus is a prerequisite for forming helices by replacing the protonated C-terminal Lys residue by Ala and a sodium cation. The combination of gas-phase vibrational spectroscopy of cryogenically cooled ions with molecular simulations based on density-functional theory (DFT) allows for detailed structure elucidation. For sodiated AcPheAla(6), we find globular rather than helical structures, as the mobile positive charge strongly interacts with the peptide backbone and disrupts secondary structure formation. Interestingly, the global minimum structure from simulation is not present in the experiment. We interpret that this is due to,high barriers involved in rearranging the peptide cation interaction that ultimately result in kinetically trapped structures being observed in the experiment.
机译：我们研究了用于研究气相中螺旋形成的肽Acpheala（5）Lyar（+），以充分了解稳定螺旋结构的力。特别是，我们解决了肽的C-末端对阳性电荷的局部固定的问题是通过通过Ala和钠阳离子替换质子化的C末端Lys残基来形成螺旋的先决条件。基于密度功能理论（DFT）的低温冷却离子的气相振动光谱与分子模拟的组合允许详细的结构阐明。对于SOIIDIAL的ACPHEALA（6），我们发现球状而不是螺旋结构，因为移动正电荷强烈与肽骨架相互作用，并破坏二级结构形成。有趣的是，实验中的模拟中的全局最小结构并不存在。我们解释了这一点是由于重新排列肽阳离子相互作用的高障碍，最终导致在实验中观察到的动力学捕获的结构。

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