Journal ArticleDOI
Probing conformational changes in proteins by mass spectrometry
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.Abstract:
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.read more
Citations
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Journal ArticleDOI
Direct monitoring of protein–protein inhibition using nano electrospray ionization mass spectrometry
Dragana Cubrilovic,Konstantin Barylyuk,Daniela Hofmann,Michal J. Walczak,Martin Gräber,Thorsten Berg,Gerhard Wider,Renato Zenobi +7 more
TL;DR: Results indicate that native ESI-MS can be widely used to study the inhibition of other relevant protein–protein interactions (PPIs), and provide a good basis for further improvement and identification of small-molecule PPI inhibitors.
Book ChapterDOI
Protein interactions probed with mass spectrometry.
Suma Kaveti,John R. Engen +1 more
TL;DR: This chapter presents several methods utilizing mass spectrometry (MS) for the analysis of protein-protein, protein-drug, and protein-metal interactions, and describes theAnalysis of protein interactions with hydrogen exchange MS methods.
Journal ArticleDOI
Chemical Synthesis of an Erythropoietin Glycoform Having a Triantennary N-Glycan: Significant Change of Biological Activity of Glycoprotein by Addition of a Small Molecular Weight Trisaccharide.
TL;DR: Efficient liquid-phase condensation reactions to prepare a sialylglycopeptide having a triantennary N-glycan prepared by the addition of a Neu5Ac-α-2,6-Gal-β-1,4-GlcNAc element to the biantennary glycan under semisynthetic conditions are demonstrated.
Journal ArticleDOI
Electrospray ionization mass spectrometry, circular dichroism and SAXS studies of the (S)-hydroxynitrile lyase from Hevea brasiliensis.
Ulf Hanefeld,Gudrun R. Stranzl,Adrie J. J. Straathof,Joseph J. Heijnen,Alexander Bergmann,Rainer Mittelbach,Otto Glatter,Christoph Kratky +7 more
TL;DR: Small angle X-ray scattering unequivocally established the enzyme to occur in solution as a dimer, presumably of the same structure as in the crystal, and showed a clear correlation between enzyme activity and unfolding as detected by ESI-MS and CD.
Journal ArticleDOI
Induction of protein conformational change inside the charged electrospray droplet
TL;DR: The protein conformational change inside the ES droplet has been driven by using acetic acid vapor in the present study and the results would help in the near future to understand the spontaneity of the conformational changes of the analyte on the millisecond timescale of phase transition in the natural way of ES process.
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