斯MoSSe/MoS2的非线性光学响应 异构体通过堆叠顺序和应变优化
Nguyen Tuan Hung1,2, Kunyan Zhang3, Vuong Van Thanh4
1Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai 980-8578, Japan.
ACS nano
|August 29, 2023
概括
研究人员优化了Janus MoSSe/MoS2异构体的非线性光学反应,发现AA堆叠显著增加了第二波生成 (SHG). 应变进一步增强了这种效果,为先进的光电子设备提供了途径.
科学领域:
- 凝聚物质物理学 凝聚物质物理学
- 材料科学 材料科学 材料科学
- 光电学是指光电子产品.
背景情况:
- 范德瓦尔斯的异构体提供可调节的电子和光学特性.
- 詹纳斯MoSSe/MoS2表现出有希望的非线性光学 (NLO) 响应.
- 二次波生成 (SHG) 是频率转换的一个关键的NLO现象.
研究的目的:
- 在Janus MoSSe/MoS2范德瓦尔斯异构体中理论上优化第二波生成 (SHG) 非线性光学响应.
- 调查堆叠顺序和应变对非线性易感性的影响 (χ(2)).
- 为实验验证提供理论预测.
主要方法:
- 使用第一原则计算与交换相关混合函数.
- 采用实时方法来模拟和计算NLO响应.
- 系统地改变堆叠顺序 (AA与AB) 并应用二维拉伸.
主要成果:
- 与AB堆叠 (χ(2) = 170 pm/V相比,AA堆叠表现出明显更高的非线性易感性 (χ(2) = 550 pm/V),这归因于被打破的反转对称性.
- 实验观测证实AA堆叠产生的峰值SHG强度是AB堆叠的四倍.
- 4%的双轴拉伸将AA (900 pm/V) 和AB (300 pm/V) 堆叠的计算 χ(2) 提高1.6倍,从而打破了C3对称性.
结论:
- 堆叠顺序和应变是优化Janus MoSSe/MoS2异质活体中SHG的关键参数.
- 在AA堆叠中被打破的反向对称性是增强非线性光学反应的关键.
- 理论预测与实验发现很好地一致,验证了设计先进光电子材料的计算方法.
相关概念视频
01:58Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
01:58Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
01:58Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...