Conformational Analysis of Large and Highly Disulfide-Stabilized Proteins by Integrating Online Electrochemical Reduction into an Optimized H/D Exchange Mass Spectrometry Workflow

Analysis of disulfide-bonded proteins by hydrogen/deuterium exchange mass spectrometry (HDX-MS) requires effective and rapid reduction of disulfide bonds before enzymatic digestion in order to increase sequence coverage. In a conventional HDX-MS workflow, disulfide bonds are reduced chemically by ad...

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Veröffentlicht in:	Analytical chemistry (Washington) 2015-09, Vol.87 (17), p.8880-8888
Hauptverfasser:	Trabjerg, Esben, Jakobsen, Rasmus U, Mysling, Simon, Christensen, Søren, Jørgensen, Thomas J. D, Rand, Kasper D
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Monoclonal - analysis Deuterium Exchange Measurement Disulfides Disulfides - chemistry Electrochemical Techniques Enzymes Exchange Hydrogen-Ion Concentration Immunoglobulin G - analysis Internet Mass Spectrometry Models, Molecular Nerve Growth Factor - analysis Online Optimization Oxidation-Reduction Protein Conformation Proteins Quenching Reduction Reduction (chemical) Temperature Workflow
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