Related ArticlesInteraction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy.
Biochemistry. 1991 Apr 9;30(14):3387-95
Authors: Snel MM, Kaptein R, de Kruijff B
The topology of apocytochrome c, the heme-free precursor of the mitochondrial protein cytochrome c, was investigated in a lipid-associated form. For this purpose photochemically induced dynamic nuclear polarization 1H nuclear magnetic resonance (CIDNP 1H NMR) spectroscopy and quenching of tryptophan and tyrosine fluorescence by acrylamide were applied to an apocytochrome c-sodium dodecyl sulfate (SDS) micellar system. A pH titration of the chemical shifts of the histidine C2 proton resonances of apocytochrome c, using conventional 1H NMR, yielded pK(a)'s of 5.9 +/- 0.1 and 6.2 +/- 0.1, which were assigned to histidine-18 and -33 and histidine-26, respectively. In the presence of SDS micelles an average pK(a) of 8.1 +/- 0.1 was obtained for all histidine C2 protons. Photo-CIDNP enhancements of the histidine, tryptophan, and tyrosine residues, contained in the intact apocytochrome c and in chemically and enzymatically prepared fragments of the precursor, were reduced in the presence of SDS micelles. Similarly, the quenching of the tryptophan fluorescence of the polypeptides by acrylamide was diminished in the presence of SDS. These results indicate the aromatic residues studied are localized in the interface of the SDS micelle.
[NMR paper] NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Related Articles NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Biochemistry. 2001 May 8;40(18):5414-21
Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR
The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used...
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11-19-2010 08:32 PM
[NMR paper] Molecular dynamics-derived conformation and intramolecular interaction analysis of th
Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
Related Articles Molecular dynamics-derived conformation and intramolecular interaction analysis of the N-acetyl-9-O-acetylneuraminic acid-containing ganglioside GD1a and NMR-based analysis of its binding to a human polyclonal immunoglobulin G fraction with selectivity for O-acetylated sialic acids.
...
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08-22-2010 02:20 PM
[NMR paper] Interaction of synthetic Alzheimer beta-protein-derived analogs with aqueous aluminum
Interaction of synthetic Alzheimer beta-protein-derived analogs with aqueous aluminum: a low-field 27Al NMR investigation.
Related Articles Interaction of synthetic Alzheimer beta-protein-derived analogs with aqueous aluminum: a low-field 27Al NMR investigation.
J Protein Chem. 1995 Nov;14(8):633-44
Authors: Vyas SB, Duffy LK
Synthetic peptides corresponding to the soluble Alzheimer beta-protein, i.e., beta 1-40 and beta 6-25, were utilized to investigate the association of aluminum using low-field 27Al nuclear magnetic resonance (NMR)...
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[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Biochemistry. 1994 Nov 8;33(44):12990-7
Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ
The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS...
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08-22-2010 03:29 AM
[NMR paper] Interaction of two complementary fragments of the bovine spinal cord myelin basic pro
Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Related Articles Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Biochemistry. 1993 Sep 21;32(37):9709-13
Authors: Hayer-Hartl M, Brophy PJ, Marsh D, Watts A
The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with...
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[BMNRC community] Freezing point of Sodium Chloride
Freezing point of Sodium Chloride
For ~ 15% sodium chloride solution, it’s freezing point is* -10 deg C.
Links:
http://chestofbooks.com/food/science/Experimental-Cookery/Freezing-Mixtures.html
http://www.engineeringtoolbox.com/sodium-chloride-water-d_1187.html
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08-22-2010 01:23 AM
[NMR paper] The mitochondrial precursor protein apocytochrome c strongly influences the order of
The mitochondrial precursor protein apocytochrome c strongly influences the order of the headgroup and acyl chains of phosphatidylserine dispersions. A 2H and 31P NMR study.
Related Articles The mitochondrial precursor protein apocytochrome c strongly influences the order of the headgroup and acyl chains of phosphatidylserine dispersions. A 2H and 31P NMR study.
Biochemistry. 1990 Mar 6;29(9):2312-21
Authors: Jordi W, de Kroon AI, Killian JA, de Kruijff B
Deuterium and phosphorus nuclear magnetic resonance techniques were used to study the...
Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl
Linear Mode
