Lysozyme revisited

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2025-01-02 DOI:10.1016/j.str.2024.12.005

Esko Oksanen

引用次数: 0

Abstract

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.

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溶菌酶重新审视

溶菌酶是晶体学家的模型系统。在本期的Structure中，Ramos等人报道了溶菌酶的原子分辨率中子结构，明确地显示了活性位点的质子化状态和氢键网络。这解决了争论了几十年的机械问题，并为蛋白质的原子细节提供了独特的视角。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

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.