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引用次数: 0
摘要
为了准备对人类碳酸酐酶 II 的 Ser2Ala 突变体的结构和功能方面进行详细的探索,我们在此提供了几乎完整的 1H、15N 和 13C 序列特异性共振赋值。位于酶 N 端区域的第 2 位丝氨酸突变为丙氨酸,大大改变了该位点的亲水性,使其成为疏水性位点。因此,有一种基本假设认为,这种突变会使该位点拒水。然而,有趣的是,对突变体结构与野生型结构的比较分析显示,两者之间的差异微乎其微。这些结果为深入研究组氨酸动力学、质子化状态及其在蛋白质与水的相互作用和催化作用中的复杂作用奠定了基础。
1H, 15N and13C resonance assignments of S2A mutant of human carbonic anhydrase II
In preparation for a detailed exploration of the structural and functional aspects of the Ser2Ala mutant of human carbonic anhydrase II, we present here almost complete sequence-specific resonance assignments for 1H, 15N, and 13C. The mutation of serine to alanine at position 2, located in the N-terminal region of the enzyme, significantly alters the hydrophilic nature of the site, rendering it hydrophobic. Consequently, there is an underlying assumption that this mutation would repel water from the site. However, intriguingly, comparative analysis of the mutant structure with the wild type reveals minimal discernible differences. These assignments serve as the basis for in-depth studies on histidine dynamics, protonation states, and its intricate role in protein-water interactions and catalysis.
期刊介绍:
Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties.
Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.