{"title":"溶菌酶重新审视","authors":"Esko Oksanen","doi":"10.1016/j.str.2024.12.005","DOIUrl":null,"url":null,"abstract":"Lysozyme is a model system for crystallographers. In this issue of <em>Structure</em>, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"23 1","pages":""},"PeriodicalIF":4.4000,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Lysozyme revisited\",\"authors\":\"Esko Oksanen\",\"doi\":\"10.1016/j.str.2024.12.005\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Lysozyme is a model system for crystallographers. In this issue of <em>Structure</em>, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.\",\"PeriodicalId\":22168,\"journal\":{\"name\":\"Structure\",\"volume\":\"23 1\",\"pages\":\"\"},\"PeriodicalIF\":4.4000,\"publicationDate\":\"2025-01-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Structure\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1016/j.str.2024.12.005\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Structure","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.str.2024.12.005","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Lysozyme is a model system for crystallographers. In this issue of Structure, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.
期刊介绍:
Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome.
In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.