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 * Research
 * Publications
 * Lab Life
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 * Home
 * Research
 * Publications
 * Lab Life
   * People
   * Opportunities
 * Downloads
 * Members Only



FRUEH
LAB



pricing


FRUEH LAB

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.




pricing



FEATURED PUBLICATIONS

Global protein dynamics as communication sensors in peptide synthetase domains

Mishra, SH., Kancherla, AK., Marincin, KA., Bouvignies, G., Nerli, S.,
Sgourakis, N., Kowling, DP., Frueh, D.P.  Science Advances, 2022 July 15;
8(28):1-15. doi: 10.1126/sciadv.abn6549 .

Dynamic thiolation-thioesterase 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

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






 * 

 * Johns Hopkins University
   School of Medicine
   Biophysics and Biophysical Chemistry
   725 N. Wolfe Street, WBSB 614
   Baltimore, MD 21205-2185
   410.955.0728


 * COMMUNITY
   
   Community We are part of the Dept. of Biophysics and Biophysical Chemistry
   Dept. at JHMI, as well as of the the Johns Hopkins Graduate Program in
   Molecular Biophysics (PMB), the Biochemistry, Cellular and Molecular Biology
   Graduate Program (BCMB), and the Chemistry-Biology Interface Graduate Program
   (CBI):
   
   Dept. of Biophysics
   PMB
   BCMB
   CBI
   The Sidney Kimmel Comprehensive Cancer Center


 * OPPORTUNITIES
   
   Information for those interested in our research:
   Please contact the PI directly for inquiries regarding research opportunities
   for undergraduates, graduate students, medical students and postdoctoral
   fellows.


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