通过氢-氘交换、功能标记和质谱法研究蛋白质结构变化。
Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.
作者信息
Englander Joan J, Del Mar Charyl, Li Will, Englander S Walter, Kim Jack S, Stranz David D, Hamuro Yoshitomo, Woods Virgil L
机构信息
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.
出版信息
Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7057-62. doi: 10.1073/pnas.1232301100. Epub 2003 May 28.
Abstract
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.
摘要
采用一种自动化的高通量、高分辨率氘交换高效液相色谱-质谱联用方法（DXMS），以扩展先前关于血红蛋白调控结构变化的位置和能量作用的氢交换研究。结果与早期高精度但范围更有限的氚交换结果相符，将分析扩展至血红蛋白两个亚基的整个序列，并识别出一些能量上重要的变化。位于接近氨基酸分辨率的变构敏感酰胺氢有助于证实局部去折叠反应的真实性，以及利用它们根据变构自由能来评估已解析的结构变化。
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