The low sensitivity of nuclear magnetic resonance (NMR) is a major bottleneck for studying the biomolecular structures of complex biomolecular assemblies. Cryogenically cooled probe technology overcomes the sensitivity limitations enabling NMR applications to challenging biomolecular systems. Here we describe solid-state NMR studies of the human blood protein vitronectin (Vn) bound to hydroxyapatite (HAP), the mineralized form of calcium phosphate, using a CryoProbe designed for magic angle...
[NMR paper] Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Related Articles Protein NMR Studies of substrate binding to human blood group A and B glycosyltransferases.
Chembiochem. 2017 Mar 03;:
Authors: Peters T, Grimm LL, Weissbach S, Flügge F, Begemann N, Palcic M
Abstract
Donor and acceptor substrate binding to human blood group A and B glycosyltransferases (GTA, GTB) has been studied by a variety of protein NMR experiments. Prior crystallographic studies have shown these enzymes to adopt an...
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03-04-2017 12:19 PM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
[NMR paper] A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
Related Articles A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
J Am Chem Soc. 2005 Jul 6;127(26):9350-1
Authors: Gibson JM, Raghunathan V, Popham JM, Stayton PS, Drobny GP
Hydroxyapatite (HAP) is the main mineral component of teeth. It is well-known that several salivary proteins and peptides bind strongly to HAP to regulate crystal growth. Interactions between a peptide derived from the N-terminal fragment of...
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12-01-2010 06:56 PM
[NMR paper] Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound t
Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound to the 447-52D antibody Fv fragment.
Related Articles Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound to the 447-52D antibody Fv fragment.
J Am Chem Soc. 2004 Apr 21;126(15):4979-90
Authors: Sharpe S, Kessler N, Anglister JA, Yau WM, Tycko R
Solid-state NMR measurements were performed on the complex of an 18-residue peptide derived from the V3 loop sequence of the gp120 envelope glycoprotein of the HIV-1 MN strain with Fv...
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11-24-2010 09:51 PM
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
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11-17-2010 11:06 PM
[NMR paper] 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Related Articles 1H NMR studies of reactions of copper complexes with human blood plasma and urine.
Biochem Pharmacol. 1992 Jan 22;43(2):137-45
Authors: Bligh SW, Boyle HA, McEwen AB, Sadler PJ, Woodham RH
Reactions of the copper complexes Cu(II)Cl2, 2-, and + (where DIPS is 3,5-diisopropylsalicylate and DMP is 2,9-dimethylphenanthroline) with human blood plasma and urine have been studied by 500 MHz 1H NMR spectroscopy, and CD spectroscopy has been used to...
Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite
Linear Mode
