Related ArticlesNMR spectroscopic study of noble gas binding into the engineered cavity of HPr(I14A) from Staphylococcus carnosus.
J Phys Chem B. 2005 Sep 29;109(38):17795-8
Authors: Nisius L, Stadler M, Kalbitzer HR, Brunner E
Xenon binding into preexisting cavities in proteins is a well-known phenomenon. Here we investigate the interaction of helium, neon, and argon with hydrophobic cavities in proteins by NMR spectroscopy. 1H and 15N chemical shifts of the I14A mutant of the histidine-containing phosphocarrier protein (HPr(I14A)) from Staphylococcus carnosus are analyzed by chemical shift mapping. Total noble gas induced chemical shifts, Delta, are calculated and compared with the corresponding values obtained using xenon as a probe atom. This comparison reveals that the same cavity is detected with both argon and xenon. Measurements using the smaller noble gases helium and neon as probe atoms do not result in comparable effects. The dependence of amide proton and nitrogen chemical shifts on the argon concentration is investigated in the range from 10 mM up to 158 mM. The average dissociation constant for argon binding into the engineered cavity is determined to be about 90 mM.
[NMR paper] Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
Related Articles Dynamics of xenon binding inside the hydrophobic cavity of pseudo-wild-type bacteriophage T4 lysozyme explored through xenon-based NMR spectroscopy.
J Am Chem Soc. 2005 Aug 24;127(33):11676-83
Authors: Desvaux H, Dubois L, Huber G, Quillin ML, Berthault P, Matthews BW
Wild-type bacteriophage T4 lysozyme contains a hydrophobic cavity with binding properties that have been...
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[NMR paper] An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mu
An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
Related Articles An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
J Am Chem Soc. 2005 Apr 13;127(14):5066-72
Authors: Choy WY, Zhou Z, Bai Y, Kay LE
15N relaxation dispersion NMR spectroscopy has been used to study exchange dynamics in a pair of mutants of Rd-apocyt b562, a redesigned four-helix-bundle protein. An analysis of the relaxation data over a range of...
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[NMR paper] NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM pr
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Related Articles NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Protein Eng. 2003 Apr;16(4):247-54
Authors: Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Drosophila GCM (glial cell missing) is a novel DNA-binding protein that determines the fate of glial precursors from the neural default to glia....
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[NMR paper] 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnos
15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Related Articles 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Protein Sci. 2000 Apr;9(4):693-703
Authors: Kalbitzer HR, Görler A, Li H, Dubovskii PV, Hengstenberg W, Kowolik C, Yamada H, Akasaka K
The pressure-induced changes in 15N enriched HPr from Staphylococcus carnosus were investigated by two-dimensional (2D) heteronuclear NMR spectroscopy at pressures ranging from...
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11-18-2010 09:15 PM
[NMR paper] NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear or
NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region...
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[NMR paper] NMR study of the molecular and electronic structure of the heme cavity in Dolabella m
NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin.
Related Articles NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin.
Biochim Biophys Acta. 1993 Jun 4;1163(3):287-96
Authors: Yamamoto Y, Suzuki T
The molecular and electronic structure of the active site of the cyanide-ligated ferric complex of the myoglobin from the mollusc Dolabella auricularia has been investigated using NMR. Analysis of nuclear Overhauser effects has revealed that...
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[NMR paper] A biochemical and NMR spectroscopic study of hydrazine in the isolated rat hepatocyte
A biochemical and NMR spectroscopic study of hydrazine in the isolated rat hepatocyte.
Related Articles A biochemical and NMR spectroscopic study of hydrazine in the isolated rat hepatocyte.
Arch Toxicol. 1992;66(9):660-8
Authors: Ghatineh S, Morgan W, Preece NE, Timbrell JA
Using isolated rat hepatocytes the biochemical effects of hydrazine have been investigated using both conventional assay techniques and high resolution proton NMR. High resolution proton NMR revealed that hydrazine caused a significant increase in alanine and lactate...
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[NMR paper] Direct measurement of agonist binding to genetically engineered peptides of the acety
Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Related Articles Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Biochemistry. 1990 Mar 13;29(10):2617-22
Authors: Fraenkel Y, Navon G, Aronheim A, Gershoni JM
Interactions of four ligands of the nicotinic acetylcholine receptor with genetically engineered peptides have been studied by NMR. A recombinant cholinergic binding...