通过直接使用双向序列相关性和替换来实现远程蛋白质序列的新对齐方法
Kejue Jia1, Mesih Kilinc1,2, Robert L Jernigan1,2
1Roy J. Carver Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA, United States.
Frontiers in bioinformatics
|October 30, 2023
概括
这项研究引入了一种新的蛋白质序列对齐方法,使用相关的残留物对作为. 这种方法增强了远程同类体检测,并改善了功能部位的识别,即使对于无序的蛋白质.
科学领域:
- 生物信息学是一种生物信息学.
- 计算生物学 计算生物学
- 结构生物学 结构生物学
背景情况:
- 了解蛋白质序列功能关系在生物信息学中至关重要.
- 序列对齐识别了保存的残留物,这些残留物往往对蛋白质结构和功能至关重要 (例如,活性位点).
- 蛋白质中相关的残留物对往往与功能性重要接触相对应,并在多个序列对齐中协调变化.
研究的目的:
- 开发一种新的序列对齐方法,利用相关的残留物对作为点.
- 为了改善远程蛋白质同类体的检测.
- 为了提高蛋白质序列对齐中的功能部位识别的准确性.
主要方法:
- 开发了一种新的序列对齐策略,该策略基于从多个序列对齐中确定的相关残留对.
- 集成的远程同类检测能力 (PROST方法) 与严格的对对序列替换分析 (Kleinjung等. 方法) 的方法.
主要成果:
- 通过使用相关的残留对来对准蛋白质序列的新方法.
- 通过整合远程同类体检测和双重替代方法,展示了改进的序列对齐.
- 提供了增强对齐的例子,从而获得更好的功能洞察力,甚至适用于无序的蛋白质.
结论:
- 新的序列对齐方法有效地使用相关的残留物对作为点.
- 结合的方法显著改善了远程同类体检测和功能站点识别.
- 这种方法为蛋白质序列对齐提供了更高的准确性,有利于研究蛋白质的功能和结构,包括诸如无序蛋白质等具有挑战性的病例.
相关概念视频
Conservation of Protein Domains Over Different Proteins
10.9K
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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K
Conservation of Protein Domains
3.1K
3.1K
Evolutionary Relationships through Genome Comparisons
5.8K
Genome comparison is one of the excellent ways to interpret the evolutionary relationships between organisms. The basic principle of genome comparison is that if two species share a common feature, it is likely encoded by the DNA sequence conserved between both species. The advent of genome sequencing technologies in the late 20th century enabled scientists to understand the concept of conservation of domains between species and helped them to deduce evolutionary relationships across diverse...
5.8K
Improving Translational Accuracy
11.4K
Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
11.4K
Protein Organization
6.5K
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....
6.5K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K


