Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry

被引：185

作者：

Englander, JJ

Del Mar, C

Li, W

Englander, SW ^{[1
]}

Kim, JS

Stranz, DD

Hamuro, Y

Woods, VL

机构：

[1] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[2] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA

[3] Sierra Analyt LLC, Modesto, CA 95355 USA

[4] ExSAR Corp, Monmouth Jct, NJ 08852 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2003年 / 100卷 / 12期

关键词：

D O I：

10.1073/pnas.1232301100

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：7057 / 7062

页数：6

共 46 条

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