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Dominique Frueh, Ph.D.
Associate Professor of Biophysics and Biophysical Chemistry
Research Interests: Use of nuclear magnetic resonance (NMR) to study modulations of protein dynamics and conformations in active enzymatic systems ...read more
Dr. Dominique Frueh is an assistant professor of biophysics and biophysical chemistry at the Johns Hopkins School of Medicine. His research focuses on non-ribosomal peptide synthetases (NRPSs) and the development of nuclear magnetic resonance (NMR) methods.
Dr. Frueh received his undergraduate degree in chemistry from Université de Lausanne in Switzerland. He earned his Ph.D. from Ecole Polytechnique Fédérale de Lausanne (EPFL) in Switzerland.
His team is currently using NMR to study modulations of protein dynamics and conformations in active enzymatic systems.
- Associate Professor of Biophysics and Biophysical Chemistry
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Research & Publications
Dr. Frueh's laboratory uses nuclear magnetic resonance (NMR) to study modulations of protein dynamics and conformations in active enzymatic systems.
Non-ribosomal peptide synthetases (NRPSs) are large enzymatic systems responsible for the biosynthesis of a wealth of secondary metabolites. To synthesize all of these remarkably diverse compounds, bacteria and fungi use a surprisingly conserved strategy: NRPSs are organized in modules, made of conserved domains, that each incorporates a dedicated substrate. Dr. Frueh and his team principally use NMR to investigate inter- and intra-domain modifications occurring during the catalytic steps of non-ribosomal peptide synthesis.
The enzymatic systems Dr. Frueh and his team investigate provide many challenges to NMR. Some of the domains or multi-domains are large, and therefore, the resulting data suffer from spectral crowding and signal losses. In addition, the proteins are subject to dynamics, which may further deteriorate the quality of the spectra. Consequently, new methods often need to be developed to overcome these challenges. The techniques provide means to assign the NMR signals to the atoms in the proteins, to measure structural constraints or to monitor dynamics. When faced with an impasse, new techniques can be designed in the lab.
Selected PublicationsView all on Pubmed
Frueh DP. "Practical aspects of NMR signal assignment in larger and challenging proteins." Prog Nucl Magn Reson Spectrosc. 2014 Apr;78:47-75. doi: 10.1016/j.pnmrs.2013.12.001. Epub 2013 Dec 15.
Harden BJ, Frueh DP. "SARA: a software environment for the analysis of relaxation data acquired with accordion spectroscopy." J Biomol NMR. 2014 Feb;58(2):83-99. doi: 10.1007/s10858-013-9807-x. Epub 2014 Jan 10.
Frueh DP, Goodrich AC, Mishra SH, Nichols SR. "NMR methods for structural studies of large monomeric and multimeric proteins." Curr Opin Struct Biol. 2013 Oct;23(5):734-9. doi: 10.1016/j.sbi.2013.06.016. Epub 2013 Jul 11.
Crenshaw CM, Wade JE, Arthanari H, Frueh D, Lane BF, Núñez ME. "Hidden in plain sight: subtle effects of the 8-oxoguanine lesion on the structure, dynamics, and thermodynamics of a 15-base pair oligodeoxynucleotide duplex." Biochemistry. 2011 Oct 4;50(39):8463-77. doi: 10.1021/bi201007t. Epub 2011 Sep 8.
Shaw BF, Arthanari H, Narovlyansky M, Durazo A, Frueh DP, Pollastri MP, Lee A, Bilgicer B, Gygi SP, Wagner G, Whitesides GM. "Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability." J Am Chem Soc. 2010 Dec 15;132(49):17411-25. doi: 10.1021/ja9067035. Epub 2010 Nov 19.