内分子CHπ吸引力介导着受约束的螺旋的形状多态性
Jinming Sun1, Zi-You Tian1, Jianbo Liu2
1State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School Shenzhen 518055 China lizg@pkusz.edu.cn.
Chemical science
|August 16, 2024
概括
研究人员利用热力学调节和CHπ相互作用探索了类组合多态性. 通过操纵分子构造,他们成功地控制了体形态,为超分子组装系统提供了新的策略.
科学领域:
- 超分子化学 超分子化学
- 生物分子自我组装的过程
- 热力学是一种热力学.
背景情况:
- 生物化学过程依赖于分子多态,其中分子采用不同的形状.
- 在像组装这样的人工系统中控制多态是具有挑战性的.
- 了解多态转换的机制对于设计自组装材料至关重要.
研究的目的:
- 探索组合中的多形态的转换机制.
- 通过热力学调节实现多态控制.
- 调查分子内CHπ吸引在体自组合中的作用.
主要方法:
- 组件的热力学调节.
- 密度函数理论 (DFT) 计算以支持构造过渡.
- 理性体设计以调节CHπ吸引概率.
主要成果:
- 确定可切换的分子内CHπ吸引力是限制多态组成在特定温度范围内的一个关键因素.
- 获得的热力学数据证实了形态转换和多态形成的原理.
- 通过改变CHπ吸引力,成功地实现了同质形态形式的选择性形成.
结论:
- 分子形状操纵对于组合中的多态性选择至关重要.
- 开发的基于模板的策略为指导多态系统中的组装路径提供了一种新的方法.
- 这项工作提供了通过热力学和非共价相互作用控制自我组装的见解.
相关概念视频
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
820
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
820
Protein Folding
7.9K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.9K
Conformations of Cyclohexane
12.3K
Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
12.3K
Intrinsically Disordered Proteins
17.7K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.7K
Chair Conformation of Cyclohexane
14.4K
The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
14.4K
Protein Organization
137.1K
Overview
137.1K


