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
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
端午完成签到,获得积分10
1秒前
高大语蕊发布了新的文献求助10
1秒前
少言发布了新的文献求助10
1秒前
2秒前
Jasper应助mumumuzzz采纳,获得10
2秒前
ha发布了新的文献求助10
2秒前
奋斗的暖阳完成签到,获得积分10
3秒前
3秒前
3秒前
if完成签到,获得积分10
4秒前
4秒前
4秒前
R_joy完成签到,获得积分10
4秒前
浮游应助gory采纳,获得10
5秒前
吃点红糖馒头完成签到,获得积分10
5秒前
huhujun发布了新的文献求助20
5秒前
5秒前
CodeCraft应助高大语蕊采纳,获得10
6秒前
fairyinn发布了新的文献求助10
7秒前
充电宝应助SKF采纳,获得10
7秒前
Ty9完成签到,获得积分10
7秒前
Fa完成签到,获得积分10
7秒前
嘿嘿啊哈完成签到,获得积分10
7秒前
科研通AI6.1应助王世凯采纳,获得10
8秒前
研友_nPbeR8发布了新的文献求助10
8秒前
8秒前
马甲甲发布了新的文献求助10
9秒前
Silole发布了新的文献求助10
10秒前
R_joy发布了新的文献求助10
10秒前
戴耿耿发布了新的文献求助10
10秒前
Nuyoah发布了新的文献求助10
11秒前
LiTianHao完成签到,获得积分10
12秒前
12秒前
12秒前
NexusExplorer应助飘逸的山彤采纳,获得10
12秒前
13秒前
SciGPT应助踏实青槐采纳,获得10
13秒前
14秒前
十二应助水天需采纳,获得10
14秒前
14秒前
高分求助中
Standards for Molecular Testing for Red Cell, Platelet, and Neutrophil Antigens, 7th edition 1000
HANDBOOK OF CHEMISTRY AND PHYSICS 106th edition 1000
ASPEN Adult Nutrition Support Core Curriculum, Fourth Edition 1000
Signals, Systems, and Signal Processing 610
脑电大模型与情感脑机接口研究--郑伟龙 500
GMP in Practice: Regulatory Expectations for the Pharmaceutical Industry 500
简明药物化学习题答案 500
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 物理 内科学 复合材料 催化作用 物理化学 光电子学 电极 细胞生物学 基因 无机化学
热门帖子
关注 科研通微信公众号,转发送积分 6298029
求助须知:如何正确求助?哪些是违规求助? 8115027
关于积分的说明 16987890
捐赠科研通 5359442
什么是DOI,文献DOI怎么找? 2847319
邀请新用户注册赠送积分活动 1824744
关于科研通互助平台的介绍 1679256