Determination of thermodynamic and kinetic properties of biomolecules by mass spectrometry

被引：30

作者：

Guelbakan, Basri ^{[2
,3
]}

Barylyuk, Konstantin ^{[2
]}

Zenobi, Renato ^{[1
,2
]}

机构：

[1] ETH, Dept Chem & Appl Biosci, CH-8093 Zurich, Switzerland

[2] ETH, Dept Chem & Appl Biosci, CH-8093 Zurich, Switzerland

[3] Hacettepe Univ, Inst Child Hlth, Div Pediat Basic Sci, TR-06100 Ankara, Turkey

来源：

CURRENT OPINION IN BIOTECHNOLOGY | 2015年 / 31卷

关键词：

ELECTRON-CAPTURE DISSOCIATION; PROTEIN-LIGAND BINDING; OF-FLIGHT INSTRUMENT; H/D EXCHANGE; HYDROGEN-EXCHANGE; GAS-PHASE; HYDROGEN/DEUTERIUM EXCHANGE; UNPURIFIED PROTEINS; SUPREX STABILITY; IONIZATION;

D O I：

10.1016/j.copbio.2014.08.003

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Over the past two decades, mass spectrometry (MS) has transformed the life sciences. The advances in understanding biomolecule structure and function by MS is progressing at an accelerated pace. MS has also largely been applied to study thermodynamic and kinetic structure of biomolecules. Herein, we highlight the recent discussions about native mass spectrometry and studies about determining stable gas phase structures, hydrogen/deuterium exchange studies about reaction kinetics and determination of binding constants of biomolecules with their ligands.

引用

页码：65 / 72

页数：8

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