Hydrophobic peptides affect binding of calmodulin and Ca2+ as explored by H/D amide exchange and mass spectrometry

Calmodulin undergoes significant conformation change in the presence of Ca2+ and hydrophobic peptides. [Display omitted] ▶ Capabilities of MS-based PLIMSTEX illustrated for calmodulin-peptide binding. ▶ Digestion of calmodulin following HDX reveals binding at component peptide level. ▶ The presence...

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Veröffentlicht in:	International journal of mass spectrometry 2011-04, Vol.302 (1-3), p.85-92
Hauptverfasser:	Sperry, Justin B., Huang, Richard Y-C., Zhu, Mei M., Rempel, Don L., Gross, Michael L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Calmodulin Hydrogen/deuterium exchange LC–MS Mastoparan Melittin Myosin light-chain kinase (MLCK) PLIMSTEX
Online-Zugang:	Volltext
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