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
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Journal ArticleDOI
A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation.
TL;DR: A two-process model in which the exchange occurs either from the protected folded state or from the unprotected unfolded state through global unfolding is suggested, indicating validity of this model for hydrogen exchange of the molten globule state.
Journal ArticleDOI
Sample Flow Rate Scan in Electrospray Ionization Mass Spectrometry Reveals Alterations in Protein Charge State Distribution
Gurpur Rakesh D. Prabhu,Gurpur Rakesh D. Prabhu,Vinoth Kumar Ponnusamy,Henryk A. Witek,Pawel L. Urban +4 more
TL;DR: The observations suggest that at low flow rates the protein molecules follow charged residue model of ionization mechanism, and at high flow rates-due to structural changes in protein molecules in large ESI droplets-the charged residue and chain ejection models can possibly co-exist.
Journal ArticleDOI
Heme-peptide/protein ions and phosphorous ligands: search for site-specific addition reactions
TL;DR: An unprecedented example of ion–molecule reaction which specifically involves a prosthetic group belonging to protein ions stands in contrast to the multiple, nonspecific interactions established by OP(OMe)3 molecules with the protonated sites of multiply charged cyt c and apomyoglobin ions.
Journal ArticleDOI
Denaturation of α‐lactalbumin and ubiquitin studied by electrospray and laser spray
TL;DR: In this article, the electrospray and laser spray mass spectra of human α-lactalbumin and bovine ubiquitin were studied, with an emphasis on the denaturation induced by laser spray.
Journal ArticleDOI
Analysis of protein folding equilibria by nano‐electrospray‐ionization mass spectrometry
TL;DR: In this article, the effect of trifluoroethanol (TFE) on a peptide and acid-unfolded cytochrome c (cyt c), monitored by circular dichroism (CD) and time-of-flight ESI-MS, illustrates the specificity of the latter technique for features of protein tertiary structure.
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