Synthesis of indoles labeled with 13C-1H and 13C-19F spin pairs is described. All syntheses utilize inexpensive carbon-13C dioxide as the 13C isotope source. Ruthenium-mediated ring-closing metathesis is the key step in construction of the 13C containing indole carbocycle. Fluorine is introduced via electrophilic fluorination at the 7-position and via palladium-mediated cross-coupling at the 4-position. Indole and fluoroindoles are viable tryptophan precursors for in vivo protein expression. We...
[NMR paper] Toward a Biorelevant Structure of Protein Kinase C Bound Modulators: Design, Synthesis, and Evaluation of Labeled Bryostatin Analogs for Analysis with REDOR NMR Spectroscopy.
Toward a Biorelevant Structure of Protein Kinase C Bound Modulators: Design, Synthesis, and Evaluation of Labeled Bryostatin Analogs for Analysis with REDOR NMR Spectroscopy.
Toward a Biorelevant Structure of Protein Kinase C Bound Modulators: Design, Synthesis, and Evaluation of Labeled Bryostatin Analogs for Analysis with REDOR NMR Spectroscopy.
J Am Chem Soc. 2015 Feb 24;
Authors: Loy BA, Lesser AB, Staveness D, Billingsley KL, Cegelski L, Wender PA
Abstract
Protein kinase C (PKC) modulators are currently of great...
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[NMR paper] Cell-free synthesis of 15N-labeled proteins for NMR studies.
Cell-free synthesis of 15N-labeled proteins for NMR studies.
Related Articles Cell-free synthesis of 15N-labeled proteins for NMR studies.
IUBMB Life. 2005 Sep;57(9):615-22
Authors: Ozawa K, Dixon NE, Otting G
Modern cell-free in vitro protein synthesis systems present powerful tools for the synthesis of isotope-labeled proteins in high yields. The production of selectively 15 N-labeled proteins from 15 N-labeled amino acids is particularly economic and yields are often sufficient to analyze the proteins very quickly by two-dimensional NMR...
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[NMR paper] Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in th
Refolding of tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study.
Related Articles Refolding of tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study.
Biochemistry. 1998 Jan 6;37(1):387-98
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase contains five tryptophan residues that are spatially distributed throughout the protein and located in different secondary structural elements....
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[NMR paper] Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Related Articles Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
J Biomol NMR. 1997 Oct;10(3):245-53
Authors: Smith DE, Su JY, Jucker FM
The power of heteronuclear NMR spectroscopy to study macromolecules and their complexes has been amply demonstrated over the last decade. The obstacle to routinely applying these techniques to the study of DNA has been the synthesis of 13C,15N-labeled DNA. Here we present a simple and efficient method to generate...
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[NMR paper] Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolat
Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
Biochemistry. 1996 Dec 24;35(51):16843-51
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase (ecDHFR, EC1.5.1.3) contains 5 tryptophan residues that have...
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[NMR paper] 19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate redu
19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Related Articles 19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Biochemistry. 1994 May 10;33(18):5502-9
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan...
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[NMR paper] 19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate redu
19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Related Articles 19F NMR spectroscopy of tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies.
Biochemistry. 1994 May 10;33(18):5502-9
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase contains five tryptophan residues distributed throughout its structure. In order to examine the regions of the protein surrounding these tryptophan...
Synthesis of (13)C/(19)F/(2)H labeled indoles for use as tryptophan precursors for protein NMR spectroscopy
Linear Mode
