在气相中控制形成键
Sunyoung Lee1, Stephen J Valentine, James P Reilly
1Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Journal of the American Chemical Society
|September 14, 2011
概括
使用真空紫外线辐射的质子结合复合物的光刺激消除了水,形成更长的氨基酸链. 这些与质子结合的二次体是形成的关键中间体,产品的特异性可以通过阻断组来控制.
科学领域:
- 物理化学 物理化学
- 化学物理 化学物理
- 生物物理化学 生物物理化学
背景情况:
- 质子结合的二极体涉及到形成途径.
- 了解键形成的动态在生物化学中至关重要.
研究的目的:
- 为了研究质子结合二次体在形成中的作用.
- 探索光激发用于受控合成的使用.
主要方法:
- 使用157nm真空紫外线辐射对质子结合复合物的光激发.
- 分析水分的排出和随后的链条延长.
- 使用碰撞诱导解离方法确认产品序列.
主要成果:
- 观察到水的消除和较长的氨基酸链的形成.
- 质子结合的二极体被确定为寿命长的中间体.
- 通过选择特定的复合物和使用阻断组来实现产品特异性.
结论:
- 质子结合二极体是光诱导形成中的稳定中间体.
- 真空紫外线辐射为合成提供了可控制的方法.
- N-或C-终端阻断组可以指导产品的特异性.
相关概念视频
Peptide Bonds
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...
Protein Folding
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...
Protein Folding
Overview
Protein Organization
Overview
Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.


