Abstract

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.

中文翻译：

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人碳酸酐酶II S2A突变体的1H、15N和13C共振归属

摘要

为了准备详细探索人碳酸酐酶 II Ser2Ala 突变体的结构和功能方面，我们在此提出¹ H、¹⁵ N 和¹³ C 的几乎完整的序列特异性共振分配。丝氨酸突变为丙氨酸位点 2 位于酶的 N 末端区域，显着改变了该位点的亲水性，使其呈现疏水性。因此，有一个潜在的假设，即这种突变会排斥该地点的水。然而，有趣的是，突变体结构与野生型的比较分析显示出最小的可辨别差异。这些任务是深入研究组氨酸动力学、质子化状态及其在蛋白质-水相互作用和催化中的复杂作用的基础。