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
The use of a commercial ESI Z-spray source for ambient ion soft landing and microdroplet reactivity experiments
Chiara Salvitti,Anna Troiani,Franco Mazzei,Cristine D’Agostino,Rosaceleste Zumpano,Chiara Baldacchini,Anna Rita Bizzarri,Alessandra Tata,Federico Pepi +8 more
TL;DR: In this article, the ability of an unmodified ESI Z-spray source to carry out ambient ion soft landing (AISL) and microdroplet reactions (MR) was tested.
Journal ArticleDOI
Electroosmotically driven solution mixing in borosilicate theta glass nESI emitters.
TL;DR: The use of electroosmosis significantly expands the flexibility of theta tips for altering solutions prior to nESI without the need for off-line sample manipulation.
Electrospray Ionization Mass Spectrometry for Determination of Noncovalent Interactions in Drug Discovery
TL;DR: Noncovalent interactions are involved in many biological processes in which biomolecules bind specifically and reversibly to a partner.
Book ChapterDOI
Protein secondary structure investigated by electrospray ionization.
Journal ArticleDOI
Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry of multimeric metalloproteins
TL;DR: In this article, five multimeric metalloprotein species were examined by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry, and isotopically resolved mass spectra were obtained for noncovalent complexes with masses ranging from 25 to 86 kDa.
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