Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Solid-state NMR of amyloid membrane interactions.
Methods Mol Biol. 2011;752:165-77
Authors: Gehman JD, Separovic F
Solid-state NMR pulse sequences often feature fewer pulses and delays than the more common solution NMR experiments. This ostensible simplicity, however, belies the care with which experimental parameters must be determined, as solid-state NMR can be much less forgiving of improper experimental set-up. This is especially true of "semi-solid" samples, such as the phospholipid vesicles...
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06-30-2011 01:24 PM
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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03-08-2011 01:40 PM
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...
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02-08-2011 06:28 PM
[NMR paper] Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I i
Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I incorporated into the active site of cyano-metmyoglobin.
Related Articles Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I incorporated into the active site of cyano-metmyoglobin.
J Biol Inorg Chem. 2005 May;10(3):283-93
Authors: Bondarenko V, Wang J, Kalish H, Balch AL, La Mar GN
In order to identify the most readily deformable portion of the heme pocket in myoglobin, equine myoglobin was reconstituted with a meso-n-butyl...
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11-25-2010 08:21 PM
[NMR paper] NMR probing of protein-protein interactions using reporter ligands and affinity tags.
NMR probing of protein-protein interactions using reporter ligands and affinity tags.
Related Articles NMR probing of protein-protein interactions using reporter ligands and affinity tags.
J Am Chem Soc. 2004 Feb 18;126(6):1636-7
Authors: Ludwiczek ML, Baminger B, Konrat R
A novel method is proposed for the detection and quantification of protein-protein interactions in solution. In this approach, one protein binding partner is tagged with a ligand binding domain, and protein-protein interaction is monitored via changes in the NMR relaxation...
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11-24-2010 09:25 PM
[NMR paper] Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mu
Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
Related Articles Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
Biochemistry. 2002 Oct 8;41(40):11954-62
Authors: Tyler R, Pelczer I, Carey J, Copié V
L75F-TrpR is a temperature-sensitive mutant of the tryptophan repressor protein of Escherichia coli in which surface-exposed residue leucine 75 in the DNA binding domain is replaced with...
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11-24-2010 08:58 PM
[NMR paper] Labeling of tyrosines in proteins with [15N]tetranitromethane, a new NMR reporter for
Labeling of tyrosines in proteins with tetranitromethane, a new NMR reporter for nitrotyrosines.
Related Articles Labeling of tyrosines in proteins with tetranitromethane, a new NMR reporter for nitrotyrosines.
Biochim Biophys Acta. 1993 Mar 26;1162(3):297-308
Authors: Skawinski WJ, Adebodun F, Cheng JT, Jordan F, Mendelsohn R
Lysozyme and ribonuclease were used as model proteins to explore the feasibility of detecting protein-bound nitrotyrosines by 15N-NMR spectroscopy. The reporter group was introduced via synthesized tetranitromethane....
Perfluoro-tert-butyl-homoserine as a sensitive (19) F NMR reporter for peptide-membrane interactions in solution.
Linear Mode
