Gian Marco Visani, Michael N. Pun, William Galvin, Eric Daniel, Kevin Borisiak, Utheri Wagura, Armita Nourmohammad
{"title":"HERMES: Holographic Equivariant neuRal network model for Mutational Effect and Stability prediction","authors":"Gian Marco Visani, Michael N. Pun, William Galvin, Eric Daniel, Kevin Borisiak, Utheri Wagura, Armita Nourmohammad","doi":"arxiv-2407.06703","DOIUrl":null,"url":null,"abstract":"Predicting the stability and fitness effects of amino acid mutations in\nproteins is a cornerstone of biological discovery and engineering. Various\nexperimental techniques have been developed to measure mutational effects,\nproviding us with extensive datasets across a diverse range of proteins. By\ntraining on these data, traditional computational modeling and more recent\nmachine learning approaches have advanced significantly in predicting\nmutational effects. Here, we introduce HERMES, a 3D rotationally equivariant\nstructure-based neural network model for mutational effect and stability\nprediction. Pre-trained to predict amino acid propensity from its surrounding\n3D structure, HERMES can be fine-tuned for mutational effects using our\nopen-source code. We present a suite of HERMES models, pre-trained with\ndifferent strategies, and fine-tuned to predict the stability effect of\nmutations. Benchmarking against other models shows that HERMES often\noutperforms or matches their performance in predicting mutational effect on\nstability, binding, and fitness. HERMES offers versatile tools for evaluating\nmutational effects and can be fine-tuned for specific predictive objectives.","PeriodicalId":501022,"journal":{"name":"arXiv - QuanBio - Biomolecules","volume":"16 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"arXiv - QuanBio - Biomolecules","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/arxiv-2407.06703","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Predicting the stability and fitness effects of amino acid mutations in
proteins is a cornerstone of biological discovery and engineering. Various
experimental techniques have been developed to measure mutational effects,
providing us with extensive datasets across a diverse range of proteins. By
training on these data, traditional computational modeling and more recent
machine learning approaches have advanced significantly in predicting
mutational effects. Here, we introduce HERMES, a 3D rotationally equivariant
structure-based neural network model for mutational effect and stability
prediction. Pre-trained to predict amino acid propensity from its surrounding
3D structure, HERMES can be fine-tuned for mutational effects using our
open-source code. We present a suite of HERMES models, pre-trained with
different strategies, and fine-tuned to predict the stability effect of
mutations. Benchmarking against other models shows that HERMES often
outperforms or matches their performance in predicting mutational effect on
stability, binding, and fitness. HERMES offers versatile tools for evaluating
mutational effects and can be fine-tuned for specific predictive objectives.