Evaluation of capillary electrophoresis-mass spectrometry for the analysis of the conformational heterogeneity of intact proteins using beta2-microglobulin as model compound
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- 作者：Laura Bertolettia ; laura.bertoletti@unipv.it" class="auth_mail" title="E-mail the corresponding author ; Julie Schapplerb ; julie.schappler@unige.ch" class="auth_mail" title="E-mail the corresponding author ; Raffaella Colomboa ; raffaella.colombo@unipv.it" class="auth_mail" title="E-mail the corresponding author ; Serge Rudazb ; serge.rudaz@unige.ch" class="auth_mail" title="E-mail the corresponding author ; Rob Haselbergc ; r.haselberg@vu.nl" class="auth_mail" title="E-mail the corresponding author ; Elena Domí ; nguez-Vegac ; e.dominguezvega@vu.nl" class="auth_mail" title="E-mail the corresponding author ; Sara Raimondid ; sara.raimondi@unipv.it" class="auth_mail" title="E-mail the corresponding author ; Govert W. Somsenc ; g.w.somsen@vu.nl" class="auth_mail" title="E-mail the corresponding author ; Ersilia De Lorenzia ; ersidelo@unipv.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：Beta2-microglobulin ; Protein conformation ; Capillary electrophoresis-mass spectrometry ; Folding ; Amyloidosis
- 刊名：Analytica Chimica Acta
- 出版年：2016
- 出版时间：16 November 2016
- 年：2016
- 卷：945
- 期：Complete
- 页码：102-109
- 全文大小：1222 K
文摘
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CE-ESI-MS is proposed for protein conformational analysis.
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The amyloidogenic protein beta2-microglobulin is used as a model.
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Protein conformers are studied under native and misfolding conditions.
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New sheathless interfacing is best suited to preserve protein structure integrity.
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CE-ESI-TOF MS reliably assigns protein forms that differ by 1 Da.