Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling-Reference-Cited by-同舟云学术

Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling

Published:2009-04-18 Issue:8 Volume:20 Page:1514-1517
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Abzalimov Rinat R.¹,Kaplan Desmond A.²,Easterling Michael L.²,Kaltashov Igor A.¹

Affiliation:

1. Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Lederle Graduate Research Tower no. 701, 01003, Amherst, MA, USA

2. Bruker Daltonics, Billerica, Massachusetts, USA

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2009.04.006

Reference17 articles.

1. Hydrogen Exchange-Mass Spectrometry

2. Crossing the phase boundary to study protein dynamics and function: combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase

3. Is There Hydrogen Scrambling in the Gas Phase? Energetic and Structural Determinants of Proton Mobility within Protein Ions

4. Transient structural disorder as a facilitator of protein-ligand binding: Native H/D exchange—Mass spectrometry study of cellular retinoic acid binding protein I

5. Structural and Dynamic Characteristics of a Partially Folded State of Ubiquitin Revealed by Hydrogen Exchange Mass Spectrometry

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