当前位置: X-MOL 学术Proteins Struct. Funct. Bioinform. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Assessment of protein model structure accuracy estimation in CASP14: Old and new challenges
Proteins: Structure, Function, and Bioinformatics ( IF 2.9 ) Pub Date : 2021-07-29 , DOI: 10.1002/prot.26192
Sohee Kwon 1 , Jonghun Won 1, 2 , Andriy Kryshtafovych 3 , Chaok Seok 1, 2
Affiliation  

In CASP, blind testing of model accuracy estimation methods has been conducted on models submitted by tertiary structure prediction servers. In CASP14, model accuracy estimation results were evaluated in terms of both global and local structure accuracy, as in the previous CASPs. Unlike the previous CASPs that did not show pronounced improvements in performance, the best single-model method (from the Baker group) showed an improved performance in CASP14, particularly in evaluating global structure accuracy when compared to both the best single-model methods in previous CASPs and the best multi-model methods in the current CASP. Although the CASP14 experiment on model accuracy estimation did not deal with the structures generated by AlphaFold2, new challenges that have arisen due to the success of AlphaFold2 are discussed.

中文翻译:

CASP14 中蛋白质模型结构精度估计的评估:新旧挑战

在CASP中,对三级结构预测服务器提交的模型进行了模型精度估计方法的盲测。在 CASP14 中,与之前的 CASP 一样,模型精度估计结果根据全局和局部结构精度进行评估。与之前的 CASP 没有表现出明显的性能改进不同,最佳单模型方法(来自 Baker 组)在 CASP14 中表现出改进的性能,特别是与之前的两种最佳单模型方法相比,在评估全局结构准确性方面CASP 和当前 CASP 中最好的多模型方法。尽管关于模型精度估计的 CASP14 实验没有处理 AlphaFold2 生成的结构,但讨论了由于 AlphaFold2 的成功而出现的新挑战。
更新日期:2021-08-05
down
wechat
bug