[NMR paper] Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite
Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite
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...
[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...
Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite - ScienceDirect.com
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