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The laboratory of John R. Engen is an academic laboratory for bioanalytical protein research and analysis by hydrogen deuterium exchange mass spectrometry (HX MS). Hydrogen exchange combined with mass spectrometry is a method of analyzing proteins to learn things about their structure and their dynamics. HX MS significantly aids our understanding of proteins and protein structure. The method relies on the exchange of deuterium for hydrogen at the backbone amide hydrogen positions in proteins. Mass spectrome

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John R. Engen Laboratory: Home | hxms.neu.edu Reviews

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The laboratory of John R. Engen is an academic laboratory for bioanalytical protein research and analysis by hydrogen deuterium exchange mass spectrometry (HX MS). Hydrogen exchange combined with mass spectrometry is a method of analyzing proteins to learn things about their structure and their dynamics. HX MS significantly aids our understanding of proteins and protein structure. The method relies on the exchange of deuterium for hydrogen at the backbone amide hydrogen positions in proteins. Mass spectrome

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John R. Engen Laboratory: Home | hxms.neu.edu Reviews

https://hxms.neu.edu

The laboratory of John R. Engen is an academic laboratory for bioanalytical protein research and analysis by hydrogen deuterium exchange mass spectrometry (HX MS). Hydrogen exchange combined with mass spectrometry is a method of analyzing proteins to learn things about their structure and their dynamics. HX MS significantly aids our understanding of proteins and protein structure. The method relies on the exchange of deuterium for hydrogen at the backbone amide hydrogen positions in proteins. Mass spectrome

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John R. Engen Laboratory: Publications 2007-2011

http://www.hxms.neu.edu/pubs/pubs2007_11.htm

John R. Engen. Antibody mechanics on a membrane-bound HIV segment essential for gp41-targeted viral neutralization. Nat Struct Mol Biol. 2011 Nov 4;18(11):1235-1243. Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins. Encyclopedia of Analytical Chemistry. 2011 DOI: 10.1002/9780470027318.a9201. Online ISBN: 9780470027318, Wiley, Robert A. Meyers, Editor-in-Chief. 1 Hydrogen Exchange in Proteins. 12 Which hydrogens and how. 122 The exchange reaction mechanism(s). 2 HX MS experiments.

2

John R. Engen Laboratory: John R. Engen

http://www.hxms.neu.edu/group/jre_bio.htm

John R. Engen. JOHN R. ENGEN, Ph.D. Professor of Bioanalytical Chemistry. Department of Chemistry and Chemical Biology. Boston, MA 02115-5000. Phone: 617.373.6046. Fax: 617.373.2855. John R. Engen is a Professor of Bioanalytical Chemistry at Northeastern University. In Boston. He also holds the position of Faculty Fellow in the Barnett Institute of Chemical and Biological Analysis. Professor Engen earned two B.S. degrees (one in molecular biology and one in biochemistry) from Union College. To probe conf...

3

John R. Engen Laboratory: Home

http://www.hxms.neu.edu/index.html

John R. Engen. Sandia National Laboratories features our long-standing collaboration with Dr. Mike Kent studying the conformation of HIV Nef at the membrane. Read the story here. Small-angle X-ray scattering reveals how the shape of the Abl kinase changes upon activating mutations. Read the ACS Editors' Choice article here. A collaboration with the Walensky Laboratory. At DFCI/HMS uncovers allosteric regulation in the MCL-1 protein. NSMB article. As part of a special issue of JASMS.

4

John R. Engen Laboratory: News Archive

http://www.hxms.neu.edu/news/news_archive.htm

John R. Engen. Lab personnel receive awards:. Early Honors Research Grant. In collaboration with Bristol-Myers Squibb, the interface between EGFR and ith hydrogen exchange MS. The results were published in JASMS. How do chaperones help proteins fold in vivo. This was one of the questions addressed by a study recently published in Cell. Greg Pirrone receives one of two 2014 travel awards from the Greater Boston Mass Spectrometry Discussion Group. To attend the ASMS meeting. In Baltimore, June 15-19. In co...

5

John R. Engen Laboratory: Current Lab News

http://www.hxms.neu.edu/news/news.htm

John R. Engen. Lab personnel receive awards:. Wolfgang Goetzinger Amgen Memorial Undergraduate Scholar Award. HX MS contributes to our understanding of how substrates are recognized and then degraded by the proteasome. Read the paper here. Not all SH3 domains are the same. Despite sequence similarity, and tertiary structure homology, the motions these domains undergo in solution can be unique. Explores Tec family SH3 domains. What makes mutants of the. Lipid transporting protein ApoA-I turn into amyloids?

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A site devoted to the study of proteins. With Hydrogen Exchange and Mass Spectrometry. How does it work? What can you learn? How big can you go? Mirror of Czech Republic). Follow the links above to explore how hydrogen exchange detected with mass spectrometry is useful for studying proteins. This website is run by. The laboratory of Prof. John R. Engen.

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John R. Engen. Our collaborative study with Tom Smithgall. On the HIV accessory protein Nef is published. In the Journal of Molecular Biology. Nef conformation changes during partner binding. We used HX MS in a multi-method study of the muscle remodeling protein GDF8, a collaboration with Scholar Rock. At Harvard Medical School and Boston Children's Hospital. Article. Together with Amy Andreotti's lab. A collaboration with Ken Westover. Updated: 02.Feb.2018.

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