探索对称性作为一个大道,用于大型蛋白质域的计算设计
Carie Fortenberry1, Elizabeth Anne Bowman, Will Proffitt
1Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235, United States.
Journal of the American Chemical Society
|October 8, 2011
概括
研究人员通过计算设计了一种对称蛋白质 (FLR),该蛋白质采用TIM-barrel超叠. 这种工程蛋白质,当分裂时,很容易形成稳定的同位素,推进蛋白质设计原则.
科学领域:
- 结构生物学是结构生物学.
- 计算式蛋白质设计
- 生物化学 生物化学
背景情况:
- 由于能量有利性,对称的同质蛋白质在自然界中很丰富.
- 拟议的对称超折叠是从基因重复和对称同位体的融合进化.
研究的目的:
- 使用ROSETTA软件,通过计算工程设计一个完全对称的蛋白质变体及其同位体.
- 研究蛋白质稳定性原理和蛋白质域的结构.
主要方法:
- 使用ROSETTA蛋白质设计软件用于计算工程.
- 结晶学被用来验证原子细节中的蛋白质对称性.
- 研究了工程蛋白质的二分化行为.
主要成果:
- 成功设计了一种可溶性单蛋白 (FLR),采用对称的 (βα) 8 TIM-桶超.
- 在二次结构排列,序列和原子细节方面,FLR表现出双重对称性.
- 工程蛋白在分裂时很容易二元化,形成预期的对称同型分子.
结论:
- FLR的计算设计表明了理解蛋白质稳定性原理的进展.
- 从较小的单元中构建更大的蛋白质域的可行策略.
- 突出了计算方法在新型蛋白质设计中的潜力.
相关概念视频
Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conservation of Protein Domains
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Folding
Overview
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
Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...


