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Back Cover: Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study (Angew. Chem. Int. Ed. 45/2016)
Author(s) -
Seo Jongcheol,
Hoffmann Waldemar,
Warnke Stephan,
Bowers Michael T.,
Pagel Kevin,
von Helden Gert
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201608030
Subject(s) - electrospray ionization , ion mobility spectrometry , gas phase , cover (algebra) , mass spectrometry , solvent , ion , chemistry , ionization , analytical chemistry (journal) , phase (matter) , spectroscopy , chromatography , organic chemistry , physics , mechanical engineering , quantum mechanics , engineering
Electrospray ionization is routinely used to release proteins into the gas phase, but it is still not clear how much of the native structure can be retained. In their Communication on page 14173 ff., G. von Helden and co‐workers present the results of a combination of ion‐mobility mass spectrometry and IR spectroscopy techniques, which indicate that, under gentle instrument conditions, gas‐phase protein ions can resemble their solution equivalents in terms of tertiary and secondary structure.