The charged arginine side chain is unique in determining many innate properties of proteins, contributing to stability and interaction surfaces, and directing allosteric regulation and enzymatic catalysis. NMR experiments can be used to reveal these processes at the molecular level, but it often requires selective insertion of carbon-13, nitrogen-15 and deuterium at defined atomic positions. We introduce a method to endow arginine residues with defined isotope patterns, combining synthetic...
[NMR paper] The synthesis of specifically isotope labelled fluorotryptophan and its use in mammalian cell-based protein expression for (19)F-NMR applications
The synthesis of specifically isotope labelled fluorotryptophan and its use in mammalian cell-based protein expression for (19)F-NMR applications
^(19)F nuclei serve as versatile sensors for detecting protein interactions and dynamics in biomolecular NMR spectroscopy. Although various methods have been developed to incorporate fluorine-containing aromatic residues into proteins using E. coli or cell-free expression techniques, similar approaches for protein production in mammalian cell lines remain limited. Here, we present a cost-effective synthetic route to obtain selectively deuterated,...
[NMR paper] Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
Related Articles Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
J Labelled Comp Radiopharm. 2017 Oct 28;:
Authors: Leeder AJ, Brown LJ, Becker-Baldus J, Mehler M, Glaubitz C, Brown RCD
Abstract
Three all-trans retinals containing multiple (13) C labels have been synthesised to enable DNP enhanced solid-state MAS NMR studies of novel...
nmrlearner
Journal club
0
10-29-2017 02:06 PM
[NMR paper] Optimization of an Escherichia coli system for cell-free synthesis of selectively N-l
Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labelled proteins for rapid analysis by NMR spectroscopy.
Related Articles Optimization of an Escherichia coli system for cell-free synthesis of selectively N-labelled proteins for rapid analysis by NMR spectroscopy.
Eur J Biochem. 2004 Oct;271(20):4084-93
Authors: Ozawa K, Headlam MJ, Schaeffer PM, Henderson BR, Dixon NE, Otting G
Cell-free protein synthesis offers rapid access to proteins that are selectively labelled with amino acids and suitable for...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] Synthesis of region-labelled proteins for NMR studies by in vitro translation of colu
Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs.
Biochimie. 1997 Jul;79(7):415-22
Authors: Pavlov MY, Freistroffer DV, Ehrenberg M
A method to synthesise region-labelled proteins for structural studies with NMR is suggested. The technique is based on in vitro...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Synthesis of region-labelled proteins for NMR studies by in vitro translation of colu
Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs.
Biochimie. 1997 Jul;79(7):415-22
Authors: Pavlov MY, Freistroffer DV, Ehrenberg M
A method to synthesise region-labelled proteins for structural studies with NMR is suggested. The technique is based on in vitro...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Conformation of the TAR RNA-arginine complex by NMR spectroscopy.
Conformation of the TAR RNA-arginine complex by NMR spectroscopy.
Related Articles Conformation of the TAR RNA-arginine complex by NMR spectroscopy.
Science. 1992 Jul 3;257(5066):76-80
Authors: Puglisi JD, Tan R, Calnan BJ, Frankel AD, Williamson JR
The messenger RNAs of human immunodeficiency virus-1 (HIV-1) have an RNA hairpin structure, TAR, at their 5' ends that contains a six-nucleotide loop and a three-nucleotide bulge. The conformations of TAR RNA and of TAR with an arginine analog specifically bound at the binding site for the viral...