The field of site-specific modification of proteins has drawn significant attentions in recent years owing to its high importance in various research areas such as the development of novel therapeutics and understanding the biochemical and cellular behaviors of proteins. The presence of a large number of reactive functional groups in the protein of interest and in the cellular environment renders the particular modification at a specific site a highly challenging task. However, with the development of sophisticated chemical methodologies it is now possible to target a specific site of a protein with a desired modification despite many challenges remain to be solved. In this context, transition metals in particular palladium mediated C-C bond forming and C-O bond cleavage reactions gained great interest owing to the unique catalytic properties of palladium. Palladium chemistry is being significantly explored for protein modifications in vitro, on cell surface and in cellular context. Very recently, palladium complexes have been also applied for the rapid deprotection of several widely utilized cysteine-protecting groups as well as in the removal of solubilizing tags to facilitate chemical protein synthesis. This minireview highlights these advances and how the accumulated knowledge of palladium chemistry in small molecules is being impressively transferred to the area of chemical protein synthesis and modification.
[NMR paper] Knight Shift in 13C NMR Resonances Confirms the Coordination of N-Heterocyclic Carbene Ligands to Water-Soluble Palladium Nanoparticles
Knight Shift in 13C NMR Resonances Confirms the Coordination of N-Heterocyclic Carbene Ligands to Water-Soluble Palladium Nanoparticles
The coordination of N-heterocyclic carbene (NHC) ligands to the surface of 3.7 nm palladium nanoparticles (PdNPs) can be unambiguously established by observation of Knight shift (KS) in the 13C resonance of the carbenic carbon. In order to validate this coordination, PdNPs with sizes ranging from 1.3 to 4.8 nm were prepared by thermal decomposition or reduction with CO of a dimethyl NHC PdII complex. NMR studies after 13CO adsorption established that the...
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[NMR paper] Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.
Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.
Related Articles Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.
Methods Mol Biol. 2016;1345:21-41
Authors: Zhang TO, Grechko M, Moran SD, Zanni MT
Abstract
This chapter provides protocols for isotope-labeling the human islet amyloid polypeptide (hIAPP or amylin) involved in type II diabetes and ?D-crystallin involved in cataract formation. Because...
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10-12-2015 01:04 AM
[NMR paper] Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Related Articles Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Chembiochem. 2014 Nov 18;
Authors: Rauthu SR, Shiao TC, André S, Miller MC, Madej E, Mayo KH, Gabius HJ, Roy R
Abstract
The emerging significance of...
[NMR paper] Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Synthesis of modified Trichinella spiralis disaccharide epitopes and a comparison of their recognition by chemical mapping and saturation transfer difference NMR.
Carbohydr Res. 2013 Nov 1;383C:1-13
Authors: Cui L, Ling CC, Sadowska J, Bundle DR
Abstract
A rat monoclonal antibody 9D4 raised against the cell surface N-glycan of the parasite Trichinella spirallis protects rats...
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11-20-2013 12:42 AM
Cell signaling, post-translational protein modifications and NMR spectroscopy
Cell signaling, post-translational protein modifications and NMR spectroscopy
Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical ...
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[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Related Articles Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
J Biomol NMR. 2005 Jul;32(3):235-41
Authors: Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA
Cell-free protein synthesis systems provide facile access to proteins in a nascent state that enables formation of soluble, native protein-protein complexes even if one of the protein components is prone...
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[NMR paper] 1H NMR structural characterization of the cytochrome c modifications in a micellar en
1H NMR structural characterization of the cytochrome c modifications in a micellar environment.
Related Articles 1H NMR structural characterization of the cytochrome c modifications in a micellar environment.
Biochemistry. 2003 Dec 30;42(51):15342-51
Authors: Chevance S, Le Rumeur E, de Certaines JD, Simonneaux G, Bondon A
The interaction of cytochrome c with micelles of sodium dodecyl sulfate was studied by proton NMR spectroscopy. The protein/micelles ratio was found to be crucial in controlling the extent of the conformational changes in...
Palladium in Chemical Protein Synthesis and Modifications
Linear Mode
