Dissociation Behavior of a TEMPO-Active Ester Cross-Linker for Peptide Structure Analysis by Free Radical Initiated Peptide Sequencing (FRIPS) in Negative ESI-MS-Reference-Cited by-同舟云学术

Dissociation Behavior of a TEMPO-Active Ester Cross-Linker for Peptide Structure Analysis by Free Radical Initiated Peptide Sequencing (FRIPS) in Negative ESI-MS

Published:2016-07-14 Issue:1 Volume:28 Page:56-68
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Hage Christoph¹,Ihling Christian H.¹,Götze Michael²,Schäfer Mathias³,Sinz Andrea¹

Affiliation:

1. Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, D-06120, Halle, Saale, Germany

2. Institute of Biochemistry, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3, D-06120, Halle, Saale, Germany

3. Department of Chemistry, University Cologne, Greinstr. 4, D-50939, Köln, Germany

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

http://link.springer.com/content/pdf/10.1007/s13361-016-1426-9.pdf

Reference44 articles.

1. The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes

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4. Mass spectrometry supported determination of protein complex structure

5. Chemical cross-linking and native mass spectrometry: A fruitful combination for structural biology

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