Analyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase-Reference-Cited by-同舟云学术

Analyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase

Published:2016-06-10 Issue:7 Volume:51 Page:504-511
ISSN:1076-5174
Container-title:Journal of Mass Spectrometry
language:en
Short-container-title:J. Mass Spectrom.

Author:

López Abraham¹²,Vilaseca Marta¹,Madurga Sergio³,Varese Monica¹,Tarragó Teresa¹⁴,Giralt Ernest¹²

Affiliation:

1. Institute for Research in Biomedicine (IRB Barcelona); The Barcelona Institute of Science and Technology; Baldiri Reixac 10 08028 Barcelona Spain

2. Department of Organic Chemistry; University of Barcelona; Martí i Franquès 1 08028 Barcelona Spain

3. Department of Physical Chemistry and Research Institute of Theoretical and Computational Chemistry (IQTCUB); University of Barcelona; Martí i Franquès 1 08028 Barcelona Spain

4. Iproteos; S.L., Barcelona Science Park, Baldiri Reixac 10 08028 Barcelona Spain

Funder

Institute for Research in Biomedicine, MINECO-FEDER

Spanish Ministry of Education and Science

Generalitat de Catalunya

IRB Barcelona Mass Spectrometry Core Facility is a ProteoRed

Publisher

Wiley

Subject

Spectroscopy

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/jms.3777/fullpdf

Reference77 articles.

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3. Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last?

4. Aspects of native proteins are retained in vacuum

5. Native mass spectrometry: a bridge between interactomics and structural biology

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