通过通过人造的疏水性腔结合,诱导短小中的α螺旋环
Christel Dolain1, Yoshiyuki Hatakeyama, Tomohisa Sawada
1Department of Applied Chemistry, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Journal of the American Chemical Society
|April 2, 2010
概括
短在水中使用人工疏水腔折叠成α螺旋结构. 和宿主之间的芳香相互作用特别推动了这种螺旋式折叠,增强了的稳定性.
科学领域:
- 生物化学 生物化学
- 超分子化学 超分子化学
- 化学生物学 化学生物学
背景情况:
- 体构成对生物功能至关重要.
- 在水溶液中诱导稳定的结构仍然具有挑战性.
- 人工疏水性腔提供了一种新的方法来稳定结构.
研究的目的:
- 为了研究在水环境中的短中诱导α螺旋形状的诱导.
- 探索芳香-芳香相互作用在质折叠中的作用.
- 为了评估的与人造疏水宿主的结合亲和力.
主要方法:
- 短的化成合成的疏水性腔.
- 谱分析以确定的二次结构 (例如,圆形二元化).
- afinity测量用于量化与宿主相互作用.
主要成果:
- 在封闭时,短成功地采用了α-螺旋形状.
- 具有两个芳香残留的体对宿主具有很高的结合亲和力.
- 分子间芳香-芳香相互作用被确定为螺旋折叠的主要驱动因素.
结论:
- 人工疏水腔可以有效地诱导和稳定水中的α-螺旋形状.
- 芳香-芳香相互作用是特定的折叠和结合的关键决定因素.
- 该策略为设计和控制结构提供了一种新的方法,用于潜在的应用.
相关概念视频
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.
Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
Protein and Protein Structure
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 can...
A protein's shape is critical to its function. For example, an enzyme can...


