不同的形状引导二自组合成晶体或水凝
M Monti1, E Scarel1, A Hassanali2
1Chem. Pharm. Sc. Dept., University of Trieste, Via L. Giorgieri 1, Trieste 34127, Italy. stener@units.it.
概括
难以预测二酸如何组合成晶体或凝. 这项研究揭示了不同的分子形状 (符合性) 引导自我组织,导致不同的结果,如水晶或凝.
科学领域:
- 超分子化学 超分子化学
- 生物物理化学 生物物理化学
背景情况:
- 预测小的自我组装,如二,成有序的结构,如水晶或凝仍然是一个重要的挑战在材料科学和化学.
- 了解控制不同自组装状态之间的过渡的因素对于设计新型功能材料至关重要.
研究的目的:
- 为了研究自我组装的 dipeptides 的构造格局.
- 阐明分子构成在引导二体自我组织向晶体或凝阶段的作用.
- 建立电子循环二元化 (ECD) 光谱和特定二形状之间的联系.
主要方法:
- 使用了*in silico* (计算) 建模和实验技术的组合.
- 分析了自组装二的电子循环二元化 (ECD) 光谱.
- 相关的光谱数据与预测的分子构造.
主要成果:
- 确定了二的独特的构造组合,这些组合可以自我组装成不同的结构.
- 证明了折叠型适合体与一种类型的自我组装 (例如,凝) 相关,而扩展型适合体与另一种类型 (例如,晶体) 相关.
- 成功破译了ECD光谱特征与驱动自我组织的主导分子构造之间的关系.
结论:
- dipeptides 的结构格局是它们自我组装结果的关键决定因素.
- 通过ECD光谱学识别的特定分子构造,作为指导晶体或凝形成的关键参与者.
- 这项工作为预测和控制基于分子构成的二自组合提供了基础.
更多相关视频
相关概念视频
Protein Folding
8.1K
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...
8.1K
Protein Organization
138.5K
Overview
138.5K
Intrinsically Disordered Proteins
17.9K
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...
17.9K
Protein and Protein Structure
79.7K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.7K
Peptide Bonds
74.8K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
74.8K
Amyloid Fibrils
9.6K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.6K


