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You have reached the web-site of the Frueh laboratory. You are welcome. Our laboratory has a dual purpose that gives rise to synergistic advances in multiple fields. We seek to unravel the molecular mechanisms of nonribosomal peptide synthetase (NRPS) domain communication, and we develop nuclear magnetic resonance (NMR) methods that facilitate studies of such challenging and dynamic proteins. Our investigations also include biochemical assays, and may be supplemented with biophysical methods such as isothermal titration calorimetry or fluorescence anisotropy. We believe that science is motivated by problem solving, and each lab member is set to solve a particular riddle that encompasses all aspects of our research. That is, a project will include wet-lab work (e.g. cloning, biochemistry), data collection and analysis (advanced NMR methods, supporting techniques), and dry-lab work (software and scripting/coding). In the end, we simultaneously advance our understanding in NRPS synthesis, push the frontiers of NMR, and help understand the role of protein dynamics in biochemistry. Enjoy your visit.

Featured Publications

Effortless assignment with 4D covariance sequential correlation maps.

Harden BJ, Mishra SH, Frueh DP. J Magn Reson. 2015 Nov;260:83-8. doi: 10.1016/j.jmr.2015.09.007. Epub 2015 Sep 21.PMID:26432397


Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts.

Goodrich AC, Harden BJ, Frueh DP. J Am Chem Soc. 2015 Sep 23;137(37):12100-9. doi: 10.1021/jacs.5b07772. Epub 2015 Sep 15. PMID: 26334259


A nuclear magnetic resonance method for probing molecular influences of substrate loading in nonribosomal peptide synthetase carrier proteins.

Goodrich AC, Frueh DP. Biochemistry. 2015 Feb 10;54(5):1154-6. doi: 10.1021/bi501433r. Epub 2015 Jan 29. PMID:25620398


Facilitated assignment of large protein NMR signals with covariance sequential spectra using spectral derivatives.

Harden BJ, Nichols SR, Frueh DP. J Am Chem Soc. 2014 Sep 24;136(38):13106-9. doi: 10.1021/ja5058407. Epub 2014 Sep 16. PMID: 25226241


Practical aspects of NMR signal assignment in larger and challenging proteins.

Frueh DP. Prog Nucl Magn Reson Spectrosc. 2014 Apr;78:47-75. doi: 10.1016/j.pnmrs.2013.12.001. Epub 2013 Dec 15. Review. PMID:24534088


SARA: a software environment for the analysis of relaxation data acquired with accordion spectroscopy.

Harden BJ, Frueh DP. J Biomol NMR. 2014 Feb;58(2):83-99. doi: 10.1007/s10858-013-9807-x. Epub 2014 Jan 10. PMID: 24408364


Dynamic thiolation-thoesterase structure of a non-ribosomal peptide synthetase.

Frueh DP, Arthanari H, Koglin A, Vosburg DA, Bennett AE, Walsh CT.  Nature, 2008 Aug 14; 454(7206):903-6. doi: 10.1038/nature07162 PMD: 18704088 Apr;78:47-75. doi: 10.1016/j.pnmrs.2013.12.001. Epub 2013 Dec 15. Review. PMID:24534088