[NMR paper] Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Biochim Biophys Acta. 2014 Dec 10;
Authors: Kumar A, Balbach J
Abstract
BACKGROUND: During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization...
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12-17-2014 09:43 PM
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Publication date: Available online 11 December 2014
Source:Biochimica et Biophysica Acta (BBA) - General Subjects</br>
Author(s): Amit Kumar , Jochen Balbach</br>
Background During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization of short-lived intermediates...
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12-12-2014 11:30 AM
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...
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11-24-2010 11:14 PM
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...
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11-20-2010 06:01 PM
[NMR paper] The mechanism of aluminum-independent G-protein activation by fluoride and magnesium.
The mechanism of aluminum-independent G-protein activation by fluoride and magnesium. 31P NMR spectroscopy and fluorescence kinetic studies.
Related Articles The mechanism of aluminum-independent G-protein activation by fluoride and magnesium. 31P NMR spectroscopy and fluorescence kinetic studies.
J Biol Chem. 1993 Feb 5;268(4):2393-402
Authors: Antonny B, Sukumar M, Bigay J, Chabre M, Higashijima T
With magnesium present, fluoride and aluminum ions activate heterotrimeric G-proteins by forming AlFx complexes that mimic the gamma phosphate of...
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08-21-2010 11:53 PM
[NMR paper] 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by
19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
Related Articles 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by Al3+ and F-.
J Biol Chem. 1991 Feb 25;266(6):3396-401
Authors: Higashijima T, Graziano MP, Suga H, Kainosho M, Gilman AG
19F and 31P NMR spectroscopy was used to study the mechanism of activation of the alpha subunits of guanine nucleotide-binding regulatory proteins (G proteins) by Al3+, Mg2+, and F-. 19F NMR spectra of solutions containing Al3+,...
Activation Mechanism of the Streptomyces Tyrosinase Assisted by the Caddie Protein
Linear Mode
