Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry
Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry
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DOI：
10.1073/pnas.1232301100
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发表时间：
2003-06-10
影响因子：
11.1
通讯作者：
Woods, VL
中科院分区：
文献类型：
--
作者：
Englander, JJ;Del Mar, C;Woods, VL
使用自动化高通量、高分辨率氘交换HPLC-MS方法（DXMS）来扩展之前关于血红蛋白中调节结构变化的位置和能量作用的氢交换研究。结果匹配早期的高度准确，但更有限的氚交换结果，扩展到两个血红蛋白亚基的整个序列的分析，并确定一些积极的重要变化。位于近氨基酸分辨率的变构敏感的酰胺氢有助于确认本地展开反应的现实和它们的用途，以评估解决的结构变化方面的变构自由能。
An automated high-throughput, high-resolution deuterium exchange HPLC-MS method (DXMS) was used to extend previous hydrogen exchange studies on the position and energetic role of regulatory structure changes in hemoglobin. The results match earlier highly accurate but much more limited tritium exchange results, extend the analysis to the entire sequence of both hemoglobin subunits, and identify some energetically important changes. Allosterically sensitive amide hydrogens located at near amino acid resolution help to confirm the reality of local unfolding reactions and their use to evaluate resolved structure changes in terms of allosteric free energy.