Related ArticlesNMR structural studies of glutathione S-transferase.
Cell Mol Life Sci. 1998 Apr;54(4):359-62
Authors: Lian LY
The use of nuclear magnetic resonance (NMR) spectroscopy for the structure determination of small proteins is now widely recognized; what is less frequently reported is the application of NMR techniques for high-resolution studies of large proteins (M(r) larger than 30 kD). We demonstrate here how an integrated approach, using heteronuclear NMR and X-ray crystallography, can provide useful and biologically important information for large protein systems. The dynamic features of the human Al-1 glutathione S-transferase and the role of the C-terminal region are being probed by NMR; in the X-ray crystal structure, the electron densities for this region of the protein are uninterpretable.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
ACS Chem Biol. 2011 May 20;6(5):419-24
Authors: Dose A, Liokatis S, Theillet FX, Selenko P, Schwarzer D
Abstract
Histone deacetylases (HDACs) and histone acetyl-transferases (HATs) are universal regulators of eukaryotic transcriptional activity and emerging therapeutic targets for human diseases. Here we describe the generation of isotope-labeled deacetylation and...
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Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
[NMR paper] NMR characterization of structure, backbone dynamics, and glutathione binding of the
NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF).
Protein Sci. 1996...
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[NMR paper] NMR studies of novel inhibitors bound to farnesyl-protein transferase.
NMR studies of novel inhibitors bound to farnesyl-protein transferase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of novel inhibitors bound to farnesyl-protein transferase.
Protein Sci. 1995 Apr;4(4):681-8
Authors: Koblan KS, Culberson JC, Desolms SJ, Giuliani EA, Mosser SD, Omer CA, Pitzenberger SM, Bogusky...
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[NMR paper] Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with
Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
Eur J Biochem. 1993 Dec 1;218(2):327-34
Authors: Bushweller JH,...
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[NMR paper] Are the histidine residues of glutathione S-transferase important in catalysis? An as
Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
Related Articles Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
J Biol Chem. 1991 Oct 15;266(29):19475-9
Authors: Zhang PH, Graminski GF, Armstrong RN
To test the proposition that a histidine residue is essential in the catalytic mechanism of glutathione S-transferase, rat liver isoenzyme 3-3...
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[NMR paper] Are the histidine residues of glutathione S-transferase important in catalysis? An as
Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
Related Articles Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
J Biol Chem. 1991 Oct 15;266(29):19475-9
Authors: Zhang PH, Graminski GF, Armstrong RN
To test the proposition that a histidine residue is essential in the catalytic mechanism of glutathione S-transferase, rat liver isoenzyme 3-3...
NMR structural studies of glutathione S-transferase.
Linear Mode
