亲爱的研友该休息了!由于当前在线用户较少,发布求助请尽量完整地填写文献信息,科研通机器人24小时在线,伴您度过漫漫科研夜!身体可是革命的本钱,早点休息,好梦!

All-atom protein sequence design based on geometric deep learning

序列(生物学) 蛋白质设计 深度学习 人工智能 计算机科学 化学 蛋白质结构 生物化学
作者
Jiale Liu,Zheng Guo,Changsheng Zhang,Luhua Lai
出处
期刊: [Cold Spring Harbor Laboratory]
被引量:2
标识
DOI:10.1101/2024.03.18.585651
摘要

Abstract The development of advanced deep learning methods has revolutionized computational protein design. Although the success rate of design has been significantly increased, the overall accuracy of de novo design remains low. Many computational sequence design approaches are devoted to recover the original sequences for given protein structures by encoding the environment of the central residue without considering atomic details of side chains. This may limit the exploration of new sequences that can fold into the same structure and restrain function design that depends on interaction details. In this study, we proposed a novel deep learning frame-work, GeoSeqBuilder, to learn the relationship between protein structure and sequence based on rotational and translational invariance by extracting the information from relative locations. We utilized geometric deep learning to fetch the spatial local geometric features from protein backbones and explicitly incorporated three-body interactions to learn the inter-residue coupling information, and then determined the central residue type. Our model recovers over 50% native residue types and simultaneously gives highly accurate prediction of side-chain conformations which gives the atomic interaction details and circumvents the dependence of protein structure prediction tools. We used the likelihood confidence log P as scoring function for sequence and structure consistence evaluation which exhibits strong correlation with TM-score, and can be applied to recognize near-native structures from protein decoys pool in protein structure prediction. We have used GeoSeqBuilder to design sequences for two proteins, including thiore-doxin and a de novo hallucinated protein. All of the 15 sequences experimentally tested can be expressed as soluble monomeric proteins with high thermal stability and correct secondary structures. We further solved one crystal structure for thioredoxin and two for the hallucinated structure and all the experimentally solved structures are in good agreement with the designed models. The two designed sequences for the hallucination structure are novel without any homologous sequences within the latest released database clust30. The ability of GeoSeqBuilder to design new sequences for given protein structures with atomic details makes it applicable, not only for de novo sequence design, but also for protein-protein interaction and functional protein design.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
Hoiden发布了新的文献求助10
1秒前
10秒前
15秒前
eric发布了新的文献求助10
18秒前
南瓜小笨111111完成签到 ,获得积分10
19秒前
王然发布了新的文献求助10
20秒前
20秒前
小二郎应助zhouyan采纳,获得10
22秒前
英俊的铭应助zk采纳,获得10
22秒前
liurong发布了新的文献求助10
27秒前
30秒前
32秒前
SciGPT应助灵巧的之瑶采纳,获得10
37秒前
zhouyan发布了新的文献求助10
39秒前
烟味完成签到,获得积分10
39秒前
美好雁卉完成签到,获得积分10
40秒前
HSJ完成签到 ,获得积分10
43秒前
思源应助liurong采纳,获得10
50秒前
徐zhipei完成签到 ,获得积分10
54秒前
可靠的大楚完成签到,获得积分20
55秒前
58秒前
58秒前
慕青应助科研通管家采纳,获得10
59秒前
舒萼完成签到,获得积分10
1分钟前
帝蒼发布了新的文献求助10
1分钟前
1分钟前
夕遇完成签到,获得积分10
1分钟前
152455发布了新的文献求助10
1分钟前
隐形曼青应助可靠的大楚采纳,获得10
1分钟前
whoknowsname完成签到,获得积分10
1分钟前
1分钟前
落后乘风完成签到,获得积分10
1分钟前
ysgzg20123完成签到,获得积分10
1分钟前
李爱国应助QQ采纳,获得10
1分钟前
小灯完成签到 ,获得积分10
1分钟前
3792338874完成签到,获得积分20
1分钟前
超帅的白易完成签到 ,获得积分10
1分钟前
1分钟前
cxw陈祥薇完成签到 ,获得积分10
1分钟前
1分钟前
高分求助中
Markov Chain Monte Carlo 10000
(应助此贴封号)【重要!!请各用户(尤其是新用户)详细阅读】【科研通的精品贴汇总】 10000
Common Foundations of American and East Asian Modernisation: From Alexander Hamilton to Junichero Koizumi 2000
Weaponeering: An Introduction Fourth Edition, Volume 1 1000
Advanced Weaponeering Fourth Edition, Volume 2 1000
Curating Socialism: A Handbook of International Art Exhibitions 1947-1989 750
悉尼大学博士学位论文,题目:Modelling and testing of one-sided stitched laminated composites. 作者:Kristopher P. Plain 700
热门求助领域 (近24小时)
化学 材料科学 医学 生物 纳米技术 工程类 有机化学 化学工程 生物化学 计算机科学 内科学 物理 复合材料 催化作用 细胞生物学 无机化学 光电子学 物理化学 电极 基因
热门帖子
关注 科研通微信公众号,转发送积分 7520874
求助须知:如何正确求助?哪些是违规求助? 9108047
关于积分的说明 19446651
捐赠科研通 7124796
什么是DOI,文献DOI怎么找? 3254804
关于科研通互助平台的介绍 2423015
邀请新用户注册赠送积分活动 2241601